Cloning, expression and functional analysis of nicotinate dehydrogenase gene cluster from Comamonas testosteroni JA1 that can hydroxylate 3-cyanopyridine
Abstract A nicotinate dehydrogenase (NaDH) gene cluster was cloned from Comamonas testosteroni JA1. The enzyme, termed $ NaDH_{JA1} $, is composed of 21, 82, and 46 kDa subunits, respectivley containing [2Fe2S], Mo(V) and cytochrome c domains. The recombinant $ NaDH_{JA1} $ can catalyze the hydroxyl...
Ausführliche Beschreibung
Autor*in: |
Yang, Yao [verfasserIn] |
---|
Format: |
Artikel |
---|---|
Sprache: |
Englisch |
Erschienen: |
2010 |
---|
Schlagwörter: |
---|
Anmerkung: |
© Springer Science+Business Media B.V. 2010 |
---|
Übergeordnetes Werk: |
Enthalten in: Biodegradation - Springer Netherlands, 1990, 21(2010), 4 vom: 02. Feb., Seite 593-602 |
---|---|
Übergeordnetes Werk: |
volume:21 ; year:2010 ; number:4 ; day:02 ; month:02 ; pages:593-602 |
Links: |
---|
DOI / URN: |
10.1007/s10532-010-9327-2 |
---|
Katalog-ID: |
OLC2050401442 |
---|
LEADER | 01000caa a22002652 4500 | ||
---|---|---|---|
001 | OLC2050401442 | ||
003 | DE-627 | ||
005 | 20230503002100.0 | ||
007 | tu | ||
008 | 200819s2010 xx ||||| 00| ||eng c | ||
024 | 7 | |a 10.1007/s10532-010-9327-2 |2 doi | |
035 | |a (DE-627)OLC2050401442 | ||
035 | |a (DE-He213)s10532-010-9327-2-p | ||
040 | |a DE-627 |b ger |c DE-627 |e rakwb | ||
041 | |a eng | ||
082 | 0 | 4 | |a 570 |a 610 |q VZ |
084 | |a 12 |2 ssgn | ||
100 | 1 | |a Yang, Yao |e verfasserin |4 aut | |
245 | 1 | 0 | |a Cloning, expression and functional analysis of nicotinate dehydrogenase gene cluster from Comamonas testosteroni JA1 that can hydroxylate 3-cyanopyridine |
264 | 1 | |c 2010 | |
336 | |a Text |b txt |2 rdacontent | ||
337 | |a ohne Hilfsmittel zu benutzen |b n |2 rdamedia | ||
338 | |a Band |b nc |2 rdacarrier | ||
500 | |a © Springer Science+Business Media B.V. 2010 | ||
520 | |a Abstract A nicotinate dehydrogenase (NaDH) gene cluster was cloned from Comamonas testosteroni JA1. The enzyme, termed $ NaDH_{JA1} $, is composed of 21, 82, and 46 kDa subunits, respectivley containing [2Fe2S], Mo(V) and cytochrome c domains. The recombinant $ NaDH_{JA1} $ can catalyze the hydroxylation of nicotinate and 3-cyanopyridine. $ NaDH_{JA1} $ protein exhibits 52.8% identity to the amino acid sequence of $ NaDH_{KT2440} $ from P. putida KT2440. Sequence alignment analysis showed that the [2Fe2S] domain in $ NaDH_{JA1} $ had a type II [2Fe-2S] motif and a type I [2Fe-2S] motif, while the same domain in $ NaDH_{KT2440} $ had only a type II [2Fe-2S] motif. $ NaDH_{KT2440} $ had an additional hypoxanthine dehydrogenase motif that $ NaDH_{JA1} $ does not have. When the small unit of $ NaDH_{JA1} $ was replaced by the small subunit from $ NaDH_{KT2440} $, the hybrid protein was able to catalyze the hydroxylation of nicotinate, but lost the ability to catalyze hydroxylation of 3-cyanopyridine. In contrast, after replacement of the small subunit of $ NaDH_{KT2440} $ with the small subunit from $ NaDH_{JA1} $, the resulting hybrid protein $ NaDH_{JAS+KTL} $ acquired the ability to hydroxylate 3-cyanopyridine. The subunits swap results indicate the [2Fe2S] motif determines the 3-cyanopyridine hydroxylation ability, which is evidently different from the previous belief that the Mo motif determines substrate specificity. | ||
650 | 4 | |a Nicotinate dehydrogenase (NaDH) | |
650 | 4 | |a Nicotinic acid | |
650 | 4 | |a 6-Hydroxynicotinic acid | |
650 | 4 | |a 3-Cyanopyridine | |
650 | 4 | |a 3-Cyano-6-hydrxoypyridine | |
700 | 1 | |a Chen, Ting |4 aut | |
700 | 1 | |a Ma, Pengjuan |4 aut | |
700 | 1 | |a Shang, Guangdong |4 aut | |
700 | 1 | |a Dai, Yijun |4 aut | |
700 | 1 | |a Yuan, Sheng |4 aut | |
773 | 0 | 8 | |i Enthalten in |t Biodegradation |d Springer Netherlands, 1990 |g 21(2010), 4 vom: 02. Feb., Seite 593-602 |w (DE-627)130929395 |w (DE-600)1056014-2 |w (DE-576)026322242 |x 0923-9820 |7 nnns |
773 | 1 | 8 | |g volume:21 |g year:2010 |g number:4 |g day:02 |g month:02 |g pages:593-602 |
856 | 4 | 1 | |u https://doi.org/10.1007/s10532-010-9327-2 |z lizenzpflichtig |3 Volltext |
912 | |a GBV_USEFLAG_A | ||
912 | |a SYSFLAG_A | ||
912 | |a GBV_OLC | ||
912 | |a SSG-OLC-UMW | ||
912 | |a SSG-OLC-TEC | ||
912 | |a SSG-OLC-CHE | ||
912 | |a GBV_ILN_70 | ||
912 | |a GBV_ILN_2016 | ||
912 | |a GBV_ILN_4082 | ||
912 | |a GBV_ILN_4219 | ||
951 | |a AR | ||
952 | |d 21 |j 2010 |e 4 |b 02 |c 02 |h 593-602 |
author_variant |
y y yy t c tc p m pm g s gs y d yd s y sy |
---|---|
matchkey_str |
article:09239820:2010----::lnnepesoaducinlnlssfioiaeeyrgnsgncutrrmoaoatsotrn |
hierarchy_sort_str |
2010 |
publishDate |
2010 |
allfields |
10.1007/s10532-010-9327-2 doi (DE-627)OLC2050401442 (DE-He213)s10532-010-9327-2-p DE-627 ger DE-627 rakwb eng 570 610 VZ 12 ssgn Yang, Yao verfasserin aut Cloning, expression and functional analysis of nicotinate dehydrogenase gene cluster from Comamonas testosteroni JA1 that can hydroxylate 3-cyanopyridine 2010 Text txt rdacontent ohne Hilfsmittel zu benutzen n rdamedia Band nc rdacarrier © Springer Science+Business Media B.V. 2010 Abstract A nicotinate dehydrogenase (NaDH) gene cluster was cloned from Comamonas testosteroni JA1. The enzyme, termed $ NaDH_{JA1} $, is composed of 21, 82, and 46 kDa subunits, respectivley containing [2Fe2S], Mo(V) and cytochrome c domains. The recombinant $ NaDH_{JA1} $ can catalyze the hydroxylation of nicotinate and 3-cyanopyridine. $ NaDH_{JA1} $ protein exhibits 52.8% identity to the amino acid sequence of $ NaDH_{KT2440} $ from P. putida KT2440. Sequence alignment analysis showed that the [2Fe2S] domain in $ NaDH_{JA1} $ had a type II [2Fe-2S] motif and a type I [2Fe-2S] motif, while the same domain in $ NaDH_{KT2440} $ had only a type II [2Fe-2S] motif. $ NaDH_{KT2440} $ had an additional hypoxanthine dehydrogenase motif that $ NaDH_{JA1} $ does not have. When the small unit of $ NaDH_{JA1} $ was replaced by the small subunit from $ NaDH_{KT2440} $, the hybrid protein was able to catalyze the hydroxylation of nicotinate, but lost the ability to catalyze hydroxylation of 3-cyanopyridine. In contrast, after replacement of the small subunit of $ NaDH_{KT2440} $ with the small subunit from $ NaDH_{JA1} $, the resulting hybrid protein $ NaDH_{JAS+KTL} $ acquired the ability to hydroxylate 3-cyanopyridine. The subunits swap results indicate the [2Fe2S] motif determines the 3-cyanopyridine hydroxylation ability, which is evidently different from the previous belief that the Mo motif determines substrate specificity. Nicotinate dehydrogenase (NaDH) Nicotinic acid 6-Hydroxynicotinic acid 3-Cyanopyridine 3-Cyano-6-hydrxoypyridine Chen, Ting aut Ma, Pengjuan aut Shang, Guangdong aut Dai, Yijun aut Yuan, Sheng aut Enthalten in Biodegradation Springer Netherlands, 1990 21(2010), 4 vom: 02. Feb., Seite 593-602 (DE-627)130929395 (DE-600)1056014-2 (DE-576)026322242 0923-9820 nnns volume:21 year:2010 number:4 day:02 month:02 pages:593-602 https://doi.org/10.1007/s10532-010-9327-2 lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_OLC SSG-OLC-UMW SSG-OLC-TEC SSG-OLC-CHE GBV_ILN_70 GBV_ILN_2016 GBV_ILN_4082 GBV_ILN_4219 AR 21 2010 4 02 02 593-602 |
spelling |
10.1007/s10532-010-9327-2 doi (DE-627)OLC2050401442 (DE-He213)s10532-010-9327-2-p DE-627 ger DE-627 rakwb eng 570 610 VZ 12 ssgn Yang, Yao verfasserin aut Cloning, expression and functional analysis of nicotinate dehydrogenase gene cluster from Comamonas testosteroni JA1 that can hydroxylate 3-cyanopyridine 2010 Text txt rdacontent ohne Hilfsmittel zu benutzen n rdamedia Band nc rdacarrier © Springer Science+Business Media B.V. 2010 Abstract A nicotinate dehydrogenase (NaDH) gene cluster was cloned from Comamonas testosteroni JA1. The enzyme, termed $ NaDH_{JA1} $, is composed of 21, 82, and 46 kDa subunits, respectivley containing [2Fe2S], Mo(V) and cytochrome c domains. The recombinant $ NaDH_{JA1} $ can catalyze the hydroxylation of nicotinate and 3-cyanopyridine. $ NaDH_{JA1} $ protein exhibits 52.8% identity to the amino acid sequence of $ NaDH_{KT2440} $ from P. putida KT2440. Sequence alignment analysis showed that the [2Fe2S] domain in $ NaDH_{JA1} $ had a type II [2Fe-2S] motif and a type I [2Fe-2S] motif, while the same domain in $ NaDH_{KT2440} $ had only a type II [2Fe-2S] motif. $ NaDH_{KT2440} $ had an additional hypoxanthine dehydrogenase motif that $ NaDH_{JA1} $ does not have. When the small unit of $ NaDH_{JA1} $ was replaced by the small subunit from $ NaDH_{KT2440} $, the hybrid protein was able to catalyze the hydroxylation of nicotinate, but lost the ability to catalyze hydroxylation of 3-cyanopyridine. In contrast, after replacement of the small subunit of $ NaDH_{KT2440} $ with the small subunit from $ NaDH_{JA1} $, the resulting hybrid protein $ NaDH_{JAS+KTL} $ acquired the ability to hydroxylate 3-cyanopyridine. The subunits swap results indicate the [2Fe2S] motif determines the 3-cyanopyridine hydroxylation ability, which is evidently different from the previous belief that the Mo motif determines substrate specificity. Nicotinate dehydrogenase (NaDH) Nicotinic acid 6-Hydroxynicotinic acid 3-Cyanopyridine 3-Cyano-6-hydrxoypyridine Chen, Ting aut Ma, Pengjuan aut Shang, Guangdong aut Dai, Yijun aut Yuan, Sheng aut Enthalten in Biodegradation Springer Netherlands, 1990 21(2010), 4 vom: 02. Feb., Seite 593-602 (DE-627)130929395 (DE-600)1056014-2 (DE-576)026322242 0923-9820 nnns volume:21 year:2010 number:4 day:02 month:02 pages:593-602 https://doi.org/10.1007/s10532-010-9327-2 lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_OLC SSG-OLC-UMW SSG-OLC-TEC SSG-OLC-CHE GBV_ILN_70 GBV_ILN_2016 GBV_ILN_4082 GBV_ILN_4219 AR 21 2010 4 02 02 593-602 |
allfields_unstemmed |
10.1007/s10532-010-9327-2 doi (DE-627)OLC2050401442 (DE-He213)s10532-010-9327-2-p DE-627 ger DE-627 rakwb eng 570 610 VZ 12 ssgn Yang, Yao verfasserin aut Cloning, expression and functional analysis of nicotinate dehydrogenase gene cluster from Comamonas testosteroni JA1 that can hydroxylate 3-cyanopyridine 2010 Text txt rdacontent ohne Hilfsmittel zu benutzen n rdamedia Band nc rdacarrier © Springer Science+Business Media B.V. 2010 Abstract A nicotinate dehydrogenase (NaDH) gene cluster was cloned from Comamonas testosteroni JA1. The enzyme, termed $ NaDH_{JA1} $, is composed of 21, 82, and 46 kDa subunits, respectivley containing [2Fe2S], Mo(V) and cytochrome c domains. The recombinant $ NaDH_{JA1} $ can catalyze the hydroxylation of nicotinate and 3-cyanopyridine. $ NaDH_{JA1} $ protein exhibits 52.8% identity to the amino acid sequence of $ NaDH_{KT2440} $ from P. putida KT2440. Sequence alignment analysis showed that the [2Fe2S] domain in $ NaDH_{JA1} $ had a type II [2Fe-2S] motif and a type I [2Fe-2S] motif, while the same domain in $ NaDH_{KT2440} $ had only a type II [2Fe-2S] motif. $ NaDH_{KT2440} $ had an additional hypoxanthine dehydrogenase motif that $ NaDH_{JA1} $ does not have. When the small unit of $ NaDH_{JA1} $ was replaced by the small subunit from $ NaDH_{KT2440} $, the hybrid protein was able to catalyze the hydroxylation of nicotinate, but lost the ability to catalyze hydroxylation of 3-cyanopyridine. In contrast, after replacement of the small subunit of $ NaDH_{KT2440} $ with the small subunit from $ NaDH_{JA1} $, the resulting hybrid protein $ NaDH_{JAS+KTL} $ acquired the ability to hydroxylate 3-cyanopyridine. The subunits swap results indicate the [2Fe2S] motif determines the 3-cyanopyridine hydroxylation ability, which is evidently different from the previous belief that the Mo motif determines substrate specificity. Nicotinate dehydrogenase (NaDH) Nicotinic acid 6-Hydroxynicotinic acid 3-Cyanopyridine 3-Cyano-6-hydrxoypyridine Chen, Ting aut Ma, Pengjuan aut Shang, Guangdong aut Dai, Yijun aut Yuan, Sheng aut Enthalten in Biodegradation Springer Netherlands, 1990 21(2010), 4 vom: 02. Feb., Seite 593-602 (DE-627)130929395 (DE-600)1056014-2 (DE-576)026322242 0923-9820 nnns volume:21 year:2010 number:4 day:02 month:02 pages:593-602 https://doi.org/10.1007/s10532-010-9327-2 lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_OLC SSG-OLC-UMW SSG-OLC-TEC SSG-OLC-CHE GBV_ILN_70 GBV_ILN_2016 GBV_ILN_4082 GBV_ILN_4219 AR 21 2010 4 02 02 593-602 |
allfieldsGer |
10.1007/s10532-010-9327-2 doi (DE-627)OLC2050401442 (DE-He213)s10532-010-9327-2-p DE-627 ger DE-627 rakwb eng 570 610 VZ 12 ssgn Yang, Yao verfasserin aut Cloning, expression and functional analysis of nicotinate dehydrogenase gene cluster from Comamonas testosteroni JA1 that can hydroxylate 3-cyanopyridine 2010 Text txt rdacontent ohne Hilfsmittel zu benutzen n rdamedia Band nc rdacarrier © Springer Science+Business Media B.V. 2010 Abstract A nicotinate dehydrogenase (NaDH) gene cluster was cloned from Comamonas testosteroni JA1. The enzyme, termed $ NaDH_{JA1} $, is composed of 21, 82, and 46 kDa subunits, respectivley containing [2Fe2S], Mo(V) and cytochrome c domains. The recombinant $ NaDH_{JA1} $ can catalyze the hydroxylation of nicotinate and 3-cyanopyridine. $ NaDH_{JA1} $ protein exhibits 52.8% identity to the amino acid sequence of $ NaDH_{KT2440} $ from P. putida KT2440. Sequence alignment analysis showed that the [2Fe2S] domain in $ NaDH_{JA1} $ had a type II [2Fe-2S] motif and a type I [2Fe-2S] motif, while the same domain in $ NaDH_{KT2440} $ had only a type II [2Fe-2S] motif. $ NaDH_{KT2440} $ had an additional hypoxanthine dehydrogenase motif that $ NaDH_{JA1} $ does not have. When the small unit of $ NaDH_{JA1} $ was replaced by the small subunit from $ NaDH_{KT2440} $, the hybrid protein was able to catalyze the hydroxylation of nicotinate, but lost the ability to catalyze hydroxylation of 3-cyanopyridine. In contrast, after replacement of the small subunit of $ NaDH_{KT2440} $ with the small subunit from $ NaDH_{JA1} $, the resulting hybrid protein $ NaDH_{JAS+KTL} $ acquired the ability to hydroxylate 3-cyanopyridine. The subunits swap results indicate the [2Fe2S] motif determines the 3-cyanopyridine hydroxylation ability, which is evidently different from the previous belief that the Mo motif determines substrate specificity. Nicotinate dehydrogenase (NaDH) Nicotinic acid 6-Hydroxynicotinic acid 3-Cyanopyridine 3-Cyano-6-hydrxoypyridine Chen, Ting aut Ma, Pengjuan aut Shang, Guangdong aut Dai, Yijun aut Yuan, Sheng aut Enthalten in Biodegradation Springer Netherlands, 1990 21(2010), 4 vom: 02. Feb., Seite 593-602 (DE-627)130929395 (DE-600)1056014-2 (DE-576)026322242 0923-9820 nnns volume:21 year:2010 number:4 day:02 month:02 pages:593-602 https://doi.org/10.1007/s10532-010-9327-2 lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_OLC SSG-OLC-UMW SSG-OLC-TEC SSG-OLC-CHE GBV_ILN_70 GBV_ILN_2016 GBV_ILN_4082 GBV_ILN_4219 AR 21 2010 4 02 02 593-602 |
allfieldsSound |
10.1007/s10532-010-9327-2 doi (DE-627)OLC2050401442 (DE-He213)s10532-010-9327-2-p DE-627 ger DE-627 rakwb eng 570 610 VZ 12 ssgn Yang, Yao verfasserin aut Cloning, expression and functional analysis of nicotinate dehydrogenase gene cluster from Comamonas testosteroni JA1 that can hydroxylate 3-cyanopyridine 2010 Text txt rdacontent ohne Hilfsmittel zu benutzen n rdamedia Band nc rdacarrier © Springer Science+Business Media B.V. 2010 Abstract A nicotinate dehydrogenase (NaDH) gene cluster was cloned from Comamonas testosteroni JA1. The enzyme, termed $ NaDH_{JA1} $, is composed of 21, 82, and 46 kDa subunits, respectivley containing [2Fe2S], Mo(V) and cytochrome c domains. The recombinant $ NaDH_{JA1} $ can catalyze the hydroxylation of nicotinate and 3-cyanopyridine. $ NaDH_{JA1} $ protein exhibits 52.8% identity to the amino acid sequence of $ NaDH_{KT2440} $ from P. putida KT2440. Sequence alignment analysis showed that the [2Fe2S] domain in $ NaDH_{JA1} $ had a type II [2Fe-2S] motif and a type I [2Fe-2S] motif, while the same domain in $ NaDH_{KT2440} $ had only a type II [2Fe-2S] motif. $ NaDH_{KT2440} $ had an additional hypoxanthine dehydrogenase motif that $ NaDH_{JA1} $ does not have. When the small unit of $ NaDH_{JA1} $ was replaced by the small subunit from $ NaDH_{KT2440} $, the hybrid protein was able to catalyze the hydroxylation of nicotinate, but lost the ability to catalyze hydroxylation of 3-cyanopyridine. In contrast, after replacement of the small subunit of $ NaDH_{KT2440} $ with the small subunit from $ NaDH_{JA1} $, the resulting hybrid protein $ NaDH_{JAS+KTL} $ acquired the ability to hydroxylate 3-cyanopyridine. The subunits swap results indicate the [2Fe2S] motif determines the 3-cyanopyridine hydroxylation ability, which is evidently different from the previous belief that the Mo motif determines substrate specificity. Nicotinate dehydrogenase (NaDH) Nicotinic acid 6-Hydroxynicotinic acid 3-Cyanopyridine 3-Cyano-6-hydrxoypyridine Chen, Ting aut Ma, Pengjuan aut Shang, Guangdong aut Dai, Yijun aut Yuan, Sheng aut Enthalten in Biodegradation Springer Netherlands, 1990 21(2010), 4 vom: 02. Feb., Seite 593-602 (DE-627)130929395 (DE-600)1056014-2 (DE-576)026322242 0923-9820 nnns volume:21 year:2010 number:4 day:02 month:02 pages:593-602 https://doi.org/10.1007/s10532-010-9327-2 lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_OLC SSG-OLC-UMW SSG-OLC-TEC SSG-OLC-CHE GBV_ILN_70 GBV_ILN_2016 GBV_ILN_4082 GBV_ILN_4219 AR 21 2010 4 02 02 593-602 |
language |
English |
source |
Enthalten in Biodegradation 21(2010), 4 vom: 02. Feb., Seite 593-602 volume:21 year:2010 number:4 day:02 month:02 pages:593-602 |
sourceStr |
Enthalten in Biodegradation 21(2010), 4 vom: 02. Feb., Seite 593-602 volume:21 year:2010 number:4 day:02 month:02 pages:593-602 |
format_phy_str_mv |
Article |
institution |
findex.gbv.de |
topic_facet |
Nicotinate dehydrogenase (NaDH) Nicotinic acid 6-Hydroxynicotinic acid 3-Cyanopyridine 3-Cyano-6-hydrxoypyridine |
dewey-raw |
570 |
isfreeaccess_bool |
false |
container_title |
Biodegradation |
authorswithroles_txt_mv |
Yang, Yao @@aut@@ Chen, Ting @@aut@@ Ma, Pengjuan @@aut@@ Shang, Guangdong @@aut@@ Dai, Yijun @@aut@@ Yuan, Sheng @@aut@@ |
publishDateDaySort_date |
2010-02-02T00:00:00Z |
hierarchy_top_id |
130929395 |
dewey-sort |
3570 |
id |
OLC2050401442 |
language_de |
englisch |
fullrecord |
<?xml version="1.0" encoding="UTF-8"?><collection xmlns="http://www.loc.gov/MARC21/slim"><record><leader>01000caa a22002652 4500</leader><controlfield tag="001">OLC2050401442</controlfield><controlfield tag="003">DE-627</controlfield><controlfield tag="005">20230503002100.0</controlfield><controlfield tag="007">tu</controlfield><controlfield tag="008">200819s2010 xx ||||| 00| ||eng c</controlfield><datafield tag="024" ind1="7" ind2=" "><subfield code="a">10.1007/s10532-010-9327-2</subfield><subfield code="2">doi</subfield></datafield><datafield tag="035" ind1=" " ind2=" "><subfield code="a">(DE-627)OLC2050401442</subfield></datafield><datafield tag="035" ind1=" " ind2=" "><subfield code="a">(DE-He213)s10532-010-9327-2-p</subfield></datafield><datafield tag="040" ind1=" " ind2=" "><subfield code="a">DE-627</subfield><subfield code="b">ger</subfield><subfield code="c">DE-627</subfield><subfield code="e">rakwb</subfield></datafield><datafield tag="041" ind1=" " ind2=" "><subfield code="a">eng</subfield></datafield><datafield tag="082" ind1="0" ind2="4"><subfield code="a">570</subfield><subfield code="a">610</subfield><subfield code="q">VZ</subfield></datafield><datafield tag="084" ind1=" " ind2=" "><subfield code="a">12</subfield><subfield code="2">ssgn</subfield></datafield><datafield tag="100" ind1="1" ind2=" "><subfield code="a">Yang, Yao</subfield><subfield code="e">verfasserin</subfield><subfield code="4">aut</subfield></datafield><datafield tag="245" ind1="1" ind2="0"><subfield code="a">Cloning, expression and functional analysis of nicotinate dehydrogenase gene cluster from Comamonas testosteroni JA1 that can hydroxylate 3-cyanopyridine</subfield></datafield><datafield tag="264" ind1=" " ind2="1"><subfield code="c">2010</subfield></datafield><datafield tag="336" ind1=" " ind2=" "><subfield code="a">Text</subfield><subfield code="b">txt</subfield><subfield code="2">rdacontent</subfield></datafield><datafield tag="337" ind1=" " ind2=" "><subfield code="a">ohne Hilfsmittel zu benutzen</subfield><subfield code="b">n</subfield><subfield code="2">rdamedia</subfield></datafield><datafield tag="338" ind1=" " ind2=" "><subfield code="a">Band</subfield><subfield code="b">nc</subfield><subfield code="2">rdacarrier</subfield></datafield><datafield tag="500" ind1=" " ind2=" "><subfield code="a">© Springer Science+Business Media B.V. 2010</subfield></datafield><datafield tag="520" ind1=" " ind2=" "><subfield code="a">Abstract A nicotinate dehydrogenase (NaDH) gene cluster was cloned from Comamonas testosteroni JA1. The enzyme, termed $ NaDH_{JA1} $, is composed of 21, 82, and 46 kDa subunits, respectivley containing [2Fe2S], Mo(V) and cytochrome c domains. The recombinant $ NaDH_{JA1} $ can catalyze the hydroxylation of nicotinate and 3-cyanopyridine. $ NaDH_{JA1} $ protein exhibits 52.8% identity to the amino acid sequence of $ NaDH_{KT2440} $ from P. putida KT2440. Sequence alignment analysis showed that the [2Fe2S] domain in $ NaDH_{JA1} $ had a type II [2Fe-2S] motif and a type I [2Fe-2S] motif, while the same domain in $ NaDH_{KT2440} $ had only a type II [2Fe-2S] motif. $ NaDH_{KT2440} $ had an additional hypoxanthine dehydrogenase motif that $ NaDH_{JA1} $ does not have. When the small unit of $ NaDH_{JA1} $ was replaced by the small subunit from $ NaDH_{KT2440} $, the hybrid protein was able to catalyze the hydroxylation of nicotinate, but lost the ability to catalyze hydroxylation of 3-cyanopyridine. In contrast, after replacement of the small subunit of $ NaDH_{KT2440} $ with the small subunit from $ NaDH_{JA1} $, the resulting hybrid protein $ NaDH_{JAS+KTL} $ acquired the ability to hydroxylate 3-cyanopyridine. The subunits swap results indicate the [2Fe2S] motif determines the 3-cyanopyridine hydroxylation ability, which is evidently different from the previous belief that the Mo motif determines substrate specificity.</subfield></datafield><datafield tag="650" ind1=" " ind2="4"><subfield code="a">Nicotinate dehydrogenase (NaDH)</subfield></datafield><datafield tag="650" ind1=" " ind2="4"><subfield code="a">Nicotinic acid</subfield></datafield><datafield tag="650" ind1=" " ind2="4"><subfield code="a">6-Hydroxynicotinic acid</subfield></datafield><datafield tag="650" ind1=" " ind2="4"><subfield code="a">3-Cyanopyridine</subfield></datafield><datafield tag="650" ind1=" " ind2="4"><subfield code="a">3-Cyano-6-hydrxoypyridine</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Chen, Ting</subfield><subfield code="4">aut</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Ma, Pengjuan</subfield><subfield code="4">aut</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Shang, Guangdong</subfield><subfield code="4">aut</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Dai, Yijun</subfield><subfield code="4">aut</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Yuan, Sheng</subfield><subfield code="4">aut</subfield></datafield><datafield tag="773" ind1="0" ind2="8"><subfield code="i">Enthalten in</subfield><subfield code="t">Biodegradation</subfield><subfield code="d">Springer Netherlands, 1990</subfield><subfield code="g">21(2010), 4 vom: 02. Feb., Seite 593-602</subfield><subfield code="w">(DE-627)130929395</subfield><subfield code="w">(DE-600)1056014-2</subfield><subfield code="w">(DE-576)026322242</subfield><subfield code="x">0923-9820</subfield><subfield code="7">nnns</subfield></datafield><datafield tag="773" ind1="1" ind2="8"><subfield code="g">volume:21</subfield><subfield code="g">year:2010</subfield><subfield code="g">number:4</subfield><subfield code="g">day:02</subfield><subfield code="g">month:02</subfield><subfield code="g">pages:593-602</subfield></datafield><datafield tag="856" ind1="4" ind2="1"><subfield code="u">https://doi.org/10.1007/s10532-010-9327-2</subfield><subfield code="z">lizenzpflichtig</subfield><subfield code="3">Volltext</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_USEFLAG_A</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">SYSFLAG_A</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_OLC</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">SSG-OLC-UMW</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">SSG-OLC-TEC</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">SSG-OLC-CHE</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_70</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_2016</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_4082</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_4219</subfield></datafield><datafield tag="951" ind1=" " ind2=" "><subfield code="a">AR</subfield></datafield><datafield tag="952" ind1=" " ind2=" "><subfield code="d">21</subfield><subfield code="j">2010</subfield><subfield code="e">4</subfield><subfield code="b">02</subfield><subfield code="c">02</subfield><subfield code="h">593-602</subfield></datafield></record></collection>
|
author |
Yang, Yao |
spellingShingle |
Yang, Yao ddc 570 ssgn 12 misc Nicotinate dehydrogenase (NaDH) misc Nicotinic acid misc 6-Hydroxynicotinic acid misc 3-Cyanopyridine misc 3-Cyano-6-hydrxoypyridine Cloning, expression and functional analysis of nicotinate dehydrogenase gene cluster from Comamonas testosteroni JA1 that can hydroxylate 3-cyanopyridine |
authorStr |
Yang, Yao |
ppnlink_with_tag_str_mv |
@@773@@(DE-627)130929395 |
format |
Article |
dewey-ones |
570 - Life sciences; biology 610 - Medicine & health |
delete_txt_mv |
keep |
author_role |
aut aut aut aut aut aut |
collection |
OLC |
remote_str |
false |
illustrated |
Not Illustrated |
issn |
0923-9820 |
topic_title |
570 610 VZ 12 ssgn Cloning, expression and functional analysis of nicotinate dehydrogenase gene cluster from Comamonas testosteroni JA1 that can hydroxylate 3-cyanopyridine Nicotinate dehydrogenase (NaDH) Nicotinic acid 6-Hydroxynicotinic acid 3-Cyanopyridine 3-Cyano-6-hydrxoypyridine |
topic |
ddc 570 ssgn 12 misc Nicotinate dehydrogenase (NaDH) misc Nicotinic acid misc 6-Hydroxynicotinic acid misc 3-Cyanopyridine misc 3-Cyano-6-hydrxoypyridine |
topic_unstemmed |
ddc 570 ssgn 12 misc Nicotinate dehydrogenase (NaDH) misc Nicotinic acid misc 6-Hydroxynicotinic acid misc 3-Cyanopyridine misc 3-Cyano-6-hydrxoypyridine |
topic_browse |
ddc 570 ssgn 12 misc Nicotinate dehydrogenase (NaDH) misc Nicotinic acid misc 6-Hydroxynicotinic acid misc 3-Cyanopyridine misc 3-Cyano-6-hydrxoypyridine |
format_facet |
Aufsätze Gedruckte Aufsätze |
format_main_str_mv |
Text Zeitschrift/Artikel |
carriertype_str_mv |
nc |
hierarchy_parent_title |
Biodegradation |
hierarchy_parent_id |
130929395 |
dewey-tens |
570 - Life sciences; biology 610 - Medicine & health |
hierarchy_top_title |
Biodegradation |
isfreeaccess_txt |
false |
familylinks_str_mv |
(DE-627)130929395 (DE-600)1056014-2 (DE-576)026322242 |
title |
Cloning, expression and functional analysis of nicotinate dehydrogenase gene cluster from Comamonas testosteroni JA1 that can hydroxylate 3-cyanopyridine |
ctrlnum |
(DE-627)OLC2050401442 (DE-He213)s10532-010-9327-2-p |
title_full |
Cloning, expression and functional analysis of nicotinate dehydrogenase gene cluster from Comamonas testosteroni JA1 that can hydroxylate 3-cyanopyridine |
author_sort |
Yang, Yao |
journal |
Biodegradation |
journalStr |
Biodegradation |
lang_code |
eng |
isOA_bool |
false |
dewey-hundreds |
500 - Science 600 - Technology |
recordtype |
marc |
publishDateSort |
2010 |
contenttype_str_mv |
txt |
container_start_page |
593 |
author_browse |
Yang, Yao Chen, Ting Ma, Pengjuan Shang, Guangdong Dai, Yijun Yuan, Sheng |
container_volume |
21 |
class |
570 610 VZ 12 ssgn |
format_se |
Aufsätze |
author-letter |
Yang, Yao |
doi_str_mv |
10.1007/s10532-010-9327-2 |
dewey-full |
570 610 |
title_sort |
cloning, expression and functional analysis of nicotinate dehydrogenase gene cluster from comamonas testosteroni ja1 that can hydroxylate 3-cyanopyridine |
title_auth |
Cloning, expression and functional analysis of nicotinate dehydrogenase gene cluster from Comamonas testosteroni JA1 that can hydroxylate 3-cyanopyridine |
abstract |
Abstract A nicotinate dehydrogenase (NaDH) gene cluster was cloned from Comamonas testosteroni JA1. The enzyme, termed $ NaDH_{JA1} $, is composed of 21, 82, and 46 kDa subunits, respectivley containing [2Fe2S], Mo(V) and cytochrome c domains. The recombinant $ NaDH_{JA1} $ can catalyze the hydroxylation of nicotinate and 3-cyanopyridine. $ NaDH_{JA1} $ protein exhibits 52.8% identity to the amino acid sequence of $ NaDH_{KT2440} $ from P. putida KT2440. Sequence alignment analysis showed that the [2Fe2S] domain in $ NaDH_{JA1} $ had a type II [2Fe-2S] motif and a type I [2Fe-2S] motif, while the same domain in $ NaDH_{KT2440} $ had only a type II [2Fe-2S] motif. $ NaDH_{KT2440} $ had an additional hypoxanthine dehydrogenase motif that $ NaDH_{JA1} $ does not have. When the small unit of $ NaDH_{JA1} $ was replaced by the small subunit from $ NaDH_{KT2440} $, the hybrid protein was able to catalyze the hydroxylation of nicotinate, but lost the ability to catalyze hydroxylation of 3-cyanopyridine. In contrast, after replacement of the small subunit of $ NaDH_{KT2440} $ with the small subunit from $ NaDH_{JA1} $, the resulting hybrid protein $ NaDH_{JAS+KTL} $ acquired the ability to hydroxylate 3-cyanopyridine. The subunits swap results indicate the [2Fe2S] motif determines the 3-cyanopyridine hydroxylation ability, which is evidently different from the previous belief that the Mo motif determines substrate specificity. © Springer Science+Business Media B.V. 2010 |
abstractGer |
Abstract A nicotinate dehydrogenase (NaDH) gene cluster was cloned from Comamonas testosteroni JA1. The enzyme, termed $ NaDH_{JA1} $, is composed of 21, 82, and 46 kDa subunits, respectivley containing [2Fe2S], Mo(V) and cytochrome c domains. The recombinant $ NaDH_{JA1} $ can catalyze the hydroxylation of nicotinate and 3-cyanopyridine. $ NaDH_{JA1} $ protein exhibits 52.8% identity to the amino acid sequence of $ NaDH_{KT2440} $ from P. putida KT2440. Sequence alignment analysis showed that the [2Fe2S] domain in $ NaDH_{JA1} $ had a type II [2Fe-2S] motif and a type I [2Fe-2S] motif, while the same domain in $ NaDH_{KT2440} $ had only a type II [2Fe-2S] motif. $ NaDH_{KT2440} $ had an additional hypoxanthine dehydrogenase motif that $ NaDH_{JA1} $ does not have. When the small unit of $ NaDH_{JA1} $ was replaced by the small subunit from $ NaDH_{KT2440} $, the hybrid protein was able to catalyze the hydroxylation of nicotinate, but lost the ability to catalyze hydroxylation of 3-cyanopyridine. In contrast, after replacement of the small subunit of $ NaDH_{KT2440} $ with the small subunit from $ NaDH_{JA1} $, the resulting hybrid protein $ NaDH_{JAS+KTL} $ acquired the ability to hydroxylate 3-cyanopyridine. The subunits swap results indicate the [2Fe2S] motif determines the 3-cyanopyridine hydroxylation ability, which is evidently different from the previous belief that the Mo motif determines substrate specificity. © Springer Science+Business Media B.V. 2010 |
abstract_unstemmed |
Abstract A nicotinate dehydrogenase (NaDH) gene cluster was cloned from Comamonas testosteroni JA1. The enzyme, termed $ NaDH_{JA1} $, is composed of 21, 82, and 46 kDa subunits, respectivley containing [2Fe2S], Mo(V) and cytochrome c domains. The recombinant $ NaDH_{JA1} $ can catalyze the hydroxylation of nicotinate and 3-cyanopyridine. $ NaDH_{JA1} $ protein exhibits 52.8% identity to the amino acid sequence of $ NaDH_{KT2440} $ from P. putida KT2440. Sequence alignment analysis showed that the [2Fe2S] domain in $ NaDH_{JA1} $ had a type II [2Fe-2S] motif and a type I [2Fe-2S] motif, while the same domain in $ NaDH_{KT2440} $ had only a type II [2Fe-2S] motif. $ NaDH_{KT2440} $ had an additional hypoxanthine dehydrogenase motif that $ NaDH_{JA1} $ does not have. When the small unit of $ NaDH_{JA1} $ was replaced by the small subunit from $ NaDH_{KT2440} $, the hybrid protein was able to catalyze the hydroxylation of nicotinate, but lost the ability to catalyze hydroxylation of 3-cyanopyridine. In contrast, after replacement of the small subunit of $ NaDH_{KT2440} $ with the small subunit from $ NaDH_{JA1} $, the resulting hybrid protein $ NaDH_{JAS+KTL} $ acquired the ability to hydroxylate 3-cyanopyridine. The subunits swap results indicate the [2Fe2S] motif determines the 3-cyanopyridine hydroxylation ability, which is evidently different from the previous belief that the Mo motif determines substrate specificity. © Springer Science+Business Media B.V. 2010 |
collection_details |
GBV_USEFLAG_A SYSFLAG_A GBV_OLC SSG-OLC-UMW SSG-OLC-TEC SSG-OLC-CHE GBV_ILN_70 GBV_ILN_2016 GBV_ILN_4082 GBV_ILN_4219 |
container_issue |
4 |
title_short |
Cloning, expression and functional analysis of nicotinate dehydrogenase gene cluster from Comamonas testosteroni JA1 that can hydroxylate 3-cyanopyridine |
url |
https://doi.org/10.1007/s10532-010-9327-2 |
remote_bool |
false |
author2 |
Chen, Ting Ma, Pengjuan Shang, Guangdong Dai, Yijun Yuan, Sheng |
author2Str |
Chen, Ting Ma, Pengjuan Shang, Guangdong Dai, Yijun Yuan, Sheng |
ppnlink |
130929395 |
mediatype_str_mv |
n |
isOA_txt |
false |
hochschulschrift_bool |
false |
doi_str |
10.1007/s10532-010-9327-2 |
up_date |
2024-07-04T01:53:07.753Z |
_version_ |
1803611524567138304 |
fullrecord_marcxml |
<?xml version="1.0" encoding="UTF-8"?><collection xmlns="http://www.loc.gov/MARC21/slim"><record><leader>01000caa a22002652 4500</leader><controlfield tag="001">OLC2050401442</controlfield><controlfield tag="003">DE-627</controlfield><controlfield tag="005">20230503002100.0</controlfield><controlfield tag="007">tu</controlfield><controlfield tag="008">200819s2010 xx ||||| 00| ||eng c</controlfield><datafield tag="024" ind1="7" ind2=" "><subfield code="a">10.1007/s10532-010-9327-2</subfield><subfield code="2">doi</subfield></datafield><datafield tag="035" ind1=" " ind2=" "><subfield code="a">(DE-627)OLC2050401442</subfield></datafield><datafield tag="035" ind1=" " ind2=" "><subfield code="a">(DE-He213)s10532-010-9327-2-p</subfield></datafield><datafield tag="040" ind1=" " ind2=" "><subfield code="a">DE-627</subfield><subfield code="b">ger</subfield><subfield code="c">DE-627</subfield><subfield code="e">rakwb</subfield></datafield><datafield tag="041" ind1=" " ind2=" "><subfield code="a">eng</subfield></datafield><datafield tag="082" ind1="0" ind2="4"><subfield code="a">570</subfield><subfield code="a">610</subfield><subfield code="q">VZ</subfield></datafield><datafield tag="084" ind1=" " ind2=" "><subfield code="a">12</subfield><subfield code="2">ssgn</subfield></datafield><datafield tag="100" ind1="1" ind2=" "><subfield code="a">Yang, Yao</subfield><subfield code="e">verfasserin</subfield><subfield code="4">aut</subfield></datafield><datafield tag="245" ind1="1" ind2="0"><subfield code="a">Cloning, expression and functional analysis of nicotinate dehydrogenase gene cluster from Comamonas testosteroni JA1 that can hydroxylate 3-cyanopyridine</subfield></datafield><datafield tag="264" ind1=" " ind2="1"><subfield code="c">2010</subfield></datafield><datafield tag="336" ind1=" " ind2=" "><subfield code="a">Text</subfield><subfield code="b">txt</subfield><subfield code="2">rdacontent</subfield></datafield><datafield tag="337" ind1=" " ind2=" "><subfield code="a">ohne Hilfsmittel zu benutzen</subfield><subfield code="b">n</subfield><subfield code="2">rdamedia</subfield></datafield><datafield tag="338" ind1=" " ind2=" "><subfield code="a">Band</subfield><subfield code="b">nc</subfield><subfield code="2">rdacarrier</subfield></datafield><datafield tag="500" ind1=" " ind2=" "><subfield code="a">© Springer Science+Business Media B.V. 2010</subfield></datafield><datafield tag="520" ind1=" " ind2=" "><subfield code="a">Abstract A nicotinate dehydrogenase (NaDH) gene cluster was cloned from Comamonas testosteroni JA1. The enzyme, termed $ NaDH_{JA1} $, is composed of 21, 82, and 46 kDa subunits, respectivley containing [2Fe2S], Mo(V) and cytochrome c domains. The recombinant $ NaDH_{JA1} $ can catalyze the hydroxylation of nicotinate and 3-cyanopyridine. $ NaDH_{JA1} $ protein exhibits 52.8% identity to the amino acid sequence of $ NaDH_{KT2440} $ from P. putida KT2440. Sequence alignment analysis showed that the [2Fe2S] domain in $ NaDH_{JA1} $ had a type II [2Fe-2S] motif and a type I [2Fe-2S] motif, while the same domain in $ NaDH_{KT2440} $ had only a type II [2Fe-2S] motif. $ NaDH_{KT2440} $ had an additional hypoxanthine dehydrogenase motif that $ NaDH_{JA1} $ does not have. When the small unit of $ NaDH_{JA1} $ was replaced by the small subunit from $ NaDH_{KT2440} $, the hybrid protein was able to catalyze the hydroxylation of nicotinate, but lost the ability to catalyze hydroxylation of 3-cyanopyridine. In contrast, after replacement of the small subunit of $ NaDH_{KT2440} $ with the small subunit from $ NaDH_{JA1} $, the resulting hybrid protein $ NaDH_{JAS+KTL} $ acquired the ability to hydroxylate 3-cyanopyridine. The subunits swap results indicate the [2Fe2S] motif determines the 3-cyanopyridine hydroxylation ability, which is evidently different from the previous belief that the Mo motif determines substrate specificity.</subfield></datafield><datafield tag="650" ind1=" " ind2="4"><subfield code="a">Nicotinate dehydrogenase (NaDH)</subfield></datafield><datafield tag="650" ind1=" " ind2="4"><subfield code="a">Nicotinic acid</subfield></datafield><datafield tag="650" ind1=" " ind2="4"><subfield code="a">6-Hydroxynicotinic acid</subfield></datafield><datafield tag="650" ind1=" " ind2="4"><subfield code="a">3-Cyanopyridine</subfield></datafield><datafield tag="650" ind1=" " ind2="4"><subfield code="a">3-Cyano-6-hydrxoypyridine</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Chen, Ting</subfield><subfield code="4">aut</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Ma, Pengjuan</subfield><subfield code="4">aut</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Shang, Guangdong</subfield><subfield code="4">aut</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Dai, Yijun</subfield><subfield code="4">aut</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Yuan, Sheng</subfield><subfield code="4">aut</subfield></datafield><datafield tag="773" ind1="0" ind2="8"><subfield code="i">Enthalten in</subfield><subfield code="t">Biodegradation</subfield><subfield code="d">Springer Netherlands, 1990</subfield><subfield code="g">21(2010), 4 vom: 02. Feb., Seite 593-602</subfield><subfield code="w">(DE-627)130929395</subfield><subfield code="w">(DE-600)1056014-2</subfield><subfield code="w">(DE-576)026322242</subfield><subfield code="x">0923-9820</subfield><subfield code="7">nnns</subfield></datafield><datafield tag="773" ind1="1" ind2="8"><subfield code="g">volume:21</subfield><subfield code="g">year:2010</subfield><subfield code="g">number:4</subfield><subfield code="g">day:02</subfield><subfield code="g">month:02</subfield><subfield code="g">pages:593-602</subfield></datafield><datafield tag="856" ind1="4" ind2="1"><subfield code="u">https://doi.org/10.1007/s10532-010-9327-2</subfield><subfield code="z">lizenzpflichtig</subfield><subfield code="3">Volltext</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_USEFLAG_A</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">SYSFLAG_A</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_OLC</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">SSG-OLC-UMW</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">SSG-OLC-TEC</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">SSG-OLC-CHE</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_70</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_2016</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_4082</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_4219</subfield></datafield><datafield tag="951" ind1=" " ind2=" "><subfield code="a">AR</subfield></datafield><datafield tag="952" ind1=" " ind2=" "><subfield code="d">21</subfield><subfield code="j">2010</subfield><subfield code="e">4</subfield><subfield code="b">02</subfield><subfield code="c">02</subfield><subfield code="h">593-602</subfield></datafield></record></collection>
|
score |
7.4001894 |