An endogenous factor enhances ferulic acid decarboxylation catalyzed by phenolic acid decarboxylase from Candida guilliermondii

Abstract The gene for a eukaryotic phenolic acid decarboxylase of Candida guilliermondii was cloned, sequenced, and expressed in Escherichia coli for the first time. The structural gene contained an open reading frame of 504 bp, corresponding to 168 amino acids with a calculated molecular mass of 19...
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Autor*in:	Huang, Hui-Kai [verfasserIn] Chen, Li-Fan [verfasserIn] Tokashiki, Masamichi [verfasserIn] Ozawa, Tadahiro [verfasserIn] Taira, Toki [verfasserIn] Ito, Susumu [verfasserIn]

Format:	E-Artikel
Sprache:	Englisch

Erschienen:	2012

Schlagwörter:	phenolic acid decarboxylase ferulic acid decarboxylase -coumaric acid decarboxylase activator

Übergeordnetes Werk:	Enthalten in: AMB express - Heidelberg : Springer, 2011, 2(2012), 1 vom: 04. Jan.
Übergeordnetes Werk:	volume:2 ; year:2012 ; number:1 ; day:04 ; month:01

Links:	Volltext

DOI / URN:	10.1186/2191-0855-2-4

Katalog-ID:	SPR031826288

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245	1	3	\|a An endogenous factor enhances ferulic acid decarboxylation catalyzed by phenolic acid decarboxylase from Candida guilliermondii
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520			\|a Abstract The gene for a eukaryotic phenolic acid decarboxylase of Candida guilliermondii was cloned, sequenced, and expressed in Escherichia coli for the first time. The structural gene contained an open reading frame of 504 bp, corresponding to 168 amino acids with a calculated molecular mass of 19,828 Da. The deduced amino sequence exhibited low similarity to those of functional phenolic acid decarboxylases previously reported from bacteria with 25-39% identity and to those of PAD1 and FDC1 proteins from Saccharomyces cerevisiae with less than 14% identity. The C. guilliermondii phenolic acid decarboxylase converted the main substrates ferulic acid and p-coumaric acid to the respective corresponding products. Surprisingly, the ultrafiltrate (Mr 10,000-cut-off) of the cell-free extract of C. guilliermondii remarkably activated the ferulic acid decarboxylation by the purified enzyme, whereas it was almost without effect on the p-coumaric acid decarboxylation. Gel-filtration chromatography of the ultrafiltrate suggested that an endogenous amino thiol-like compound with a molecular weight greater than Mr 1,400 was responsible for the activation.
650		4	\|a phenolic acid decarboxylase \|7 (dpeaa)DE-He213
650		4	\|a ferulic acid decarboxylase \|7 (dpeaa)DE-He213
650		4	\|a -coumaric acid decarboxylase \|7 (dpeaa)DE-He213
650		4	\|a activator \|7 (dpeaa)DE-He213
700	1		\|a Chen, Li-Fan \|e verfasserin \|4 aut
700	1		\|a Tokashiki, Masamichi \|e verfasserin \|4 aut
700	1		\|a Ozawa, Tadahiro \|e verfasserin \|4 aut
700	1		\|a Taira, Toki \|e verfasserin \|4 aut
700	1		\|a Ito, Susumu \|e verfasserin \|4 aut
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856	4	0	\|u https://dx.doi.org/10.1186/2191-0855-2-4 \|z lizenzpflichtig \|3 Volltext
912			\|a GBV_USEFLAG_A
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912			\|a GBV_ILN_23
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912			\|a GBV_ILN_31
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912			\|a GBV_ILN_40
912			\|a GBV_ILN_62
912			\|a GBV_ILN_63
912			\|a GBV_ILN_65
912			\|a GBV_ILN_69
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912			\|a GBV_ILN_73
912			\|a GBV_ILN_74
912			\|a GBV_ILN_95
912			\|a GBV_ILN_105
912			\|a GBV_ILN_110
912			\|a GBV_ILN_151
912			\|a GBV_ILN_161
912			\|a GBV_ILN_170
912			\|a GBV_ILN_213
912			\|a GBV_ILN_230
912			\|a GBV_ILN_285
912			\|a GBV_ILN_293
912			\|a GBV_ILN_602
912			\|a GBV_ILN_2014
912			\|a GBV_ILN_4012
912			\|a GBV_ILN_4037
912			\|a GBV_ILN_4112
912			\|a GBV_ILN_4125
912			\|a GBV_ILN_4126
912			\|a GBV_ILN_4249
912			\|a GBV_ILN_4305
912			\|a GBV_ILN_4306
912			\|a GBV_ILN_4307
912			\|a GBV_ILN_4313
912			\|a GBV_ILN_4322
912			\|a GBV_ILN_4323
912			\|a GBV_ILN_4324
912			\|a GBV_ILN_4325
912			\|a GBV_ILN_4338
912			\|a GBV_ILN_4367
912			\|a GBV_ILN_4700
936	b	k	\|a 58.30 \|q ASE
951			\|a AR
952			\|d 2 \|j 2012 \|e 1 \|b 04 \|c 01

Indexfelder

author_variant	h k h hkh l f c lfc m t mt t o to t t tt s i si
matchkey_str	article:21910855:2012----::nnoeosatrnacseuiaidcroyainaayebpeoiaidcroy
hierarchy_sort_str	2012
bklnumber	58.30
publishDate	2012
allfields	10.1186/2191-0855-2-4 doi (DE-627)SPR031826288 (SPR)2191-0855-2-4-e DE-627 ger DE-627 rakwb eng 570 ASE 58.30 bkl Huang, Hui-Kai verfasserin aut An endogenous factor enhances ferulic acid decarboxylation catalyzed by phenolic acid decarboxylase from Candida guilliermondii 2012 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Abstract The gene for a eukaryotic phenolic acid decarboxylase of Candida guilliermondii was cloned, sequenced, and expressed in Escherichia coli for the first time. The structural gene contained an open reading frame of 504 bp, corresponding to 168 amino acids with a calculated molecular mass of 19,828 Da. The deduced amino sequence exhibited low similarity to those of functional phenolic acid decarboxylases previously reported from bacteria with 25-39% identity and to those of PAD1 and FDC1 proteins from Saccharomyces cerevisiae with less than 14% identity. The C. guilliermondii phenolic acid decarboxylase converted the main substrates ferulic acid and p-coumaric acid to the respective corresponding products. Surprisingly, the ultrafiltrate (Mr 10,000-cut-off) of the cell-free extract of C. guilliermondii remarkably activated the ferulic acid decarboxylation by the purified enzyme, whereas it was almost without effect on the p-coumaric acid decarboxylation. Gel-filtration chromatography of the ultrafiltrate suggested that an endogenous amino thiol-like compound with a molecular weight greater than Mr 1,400 was responsible for the activation. phenolic acid decarboxylase (dpeaa)DE-He213 ferulic acid decarboxylase (dpeaa)DE-He213 -coumaric acid decarboxylase (dpeaa)DE-He213 activator (dpeaa)DE-He213 Chen, Li-Fan verfasserin aut Tokashiki, Masamichi verfasserin aut Ozawa, Tadahiro verfasserin aut Taira, Toki verfasserin aut Ito, Susumu verfasserin aut Enthalten in AMB express Heidelberg : Springer, 2011 2(2012), 1 vom: 04. Jan. (DE-627)665672926 (DE-600)2621432-5 2191-0855 nnns volume:2 year:2012 number:1 day:04 month:01 https://dx.doi.org/10.1186/2191-0855-2-4 lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_SPRINGER SSG-OLC-PHA GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_39 GBV_ILN_40 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_74 GBV_ILN_95 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_161 GBV_ILN_170 GBV_ILN_213 GBV_ILN_230 GBV_ILN_285 GBV_ILN_293 GBV_ILN_602 GBV_ILN_2014 GBV_ILN_4012 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4249 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4700 58.30 ASE AR 2 2012 1 04 01
spelling	10.1186/2191-0855-2-4 doi (DE-627)SPR031826288 (SPR)2191-0855-2-4-e DE-627 ger DE-627 rakwb eng 570 ASE 58.30 bkl Huang, Hui-Kai verfasserin aut An endogenous factor enhances ferulic acid decarboxylation catalyzed by phenolic acid decarboxylase from Candida guilliermondii 2012 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Abstract The gene for a eukaryotic phenolic acid decarboxylase of Candida guilliermondii was cloned, sequenced, and expressed in Escherichia coli for the first time. The structural gene contained an open reading frame of 504 bp, corresponding to 168 amino acids with a calculated molecular mass of 19,828 Da. The deduced amino sequence exhibited low similarity to those of functional phenolic acid decarboxylases previously reported from bacteria with 25-39% identity and to those of PAD1 and FDC1 proteins from Saccharomyces cerevisiae with less than 14% identity. The C. guilliermondii phenolic acid decarboxylase converted the main substrates ferulic acid and p-coumaric acid to the respective corresponding products. Surprisingly, the ultrafiltrate (Mr 10,000-cut-off) of the cell-free extract of C. guilliermondii remarkably activated the ferulic acid decarboxylation by the purified enzyme, whereas it was almost without effect on the p-coumaric acid decarboxylation. Gel-filtration chromatography of the ultrafiltrate suggested that an endogenous amino thiol-like compound with a molecular weight greater than Mr 1,400 was responsible for the activation. phenolic acid decarboxylase (dpeaa)DE-He213 ferulic acid decarboxylase (dpeaa)DE-He213 -coumaric acid decarboxylase (dpeaa)DE-He213 activator (dpeaa)DE-He213 Chen, Li-Fan verfasserin aut Tokashiki, Masamichi verfasserin aut Ozawa, Tadahiro verfasserin aut Taira, Toki verfasserin aut Ito, Susumu verfasserin aut Enthalten in AMB express Heidelberg : Springer, 2011 2(2012), 1 vom: 04. Jan. (DE-627)665672926 (DE-600)2621432-5 2191-0855 nnns volume:2 year:2012 number:1 day:04 month:01 https://dx.doi.org/10.1186/2191-0855-2-4 lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_SPRINGER SSG-OLC-PHA GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_39 GBV_ILN_40 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_74 GBV_ILN_95 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_161 GBV_ILN_170 GBV_ILN_213 GBV_ILN_230 GBV_ILN_285 GBV_ILN_293 GBV_ILN_602 GBV_ILN_2014 GBV_ILN_4012 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4249 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4700 58.30 ASE AR 2 2012 1 04 01
allfields_unstemmed	10.1186/2191-0855-2-4 doi (DE-627)SPR031826288 (SPR)2191-0855-2-4-e DE-627 ger DE-627 rakwb eng 570 ASE 58.30 bkl Huang, Hui-Kai verfasserin aut An endogenous factor enhances ferulic acid decarboxylation catalyzed by phenolic acid decarboxylase from Candida guilliermondii 2012 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Abstract The gene for a eukaryotic phenolic acid decarboxylase of Candida guilliermondii was cloned, sequenced, and expressed in Escherichia coli for the first time. The structural gene contained an open reading frame of 504 bp, corresponding to 168 amino acids with a calculated molecular mass of 19,828 Da. The deduced amino sequence exhibited low similarity to those of functional phenolic acid decarboxylases previously reported from bacteria with 25-39% identity and to those of PAD1 and FDC1 proteins from Saccharomyces cerevisiae with less than 14% identity. The C. guilliermondii phenolic acid decarboxylase converted the main substrates ferulic acid and p-coumaric acid to the respective corresponding products. Surprisingly, the ultrafiltrate (Mr 10,000-cut-off) of the cell-free extract of C. guilliermondii remarkably activated the ferulic acid decarboxylation by the purified enzyme, whereas it was almost without effect on the p-coumaric acid decarboxylation. Gel-filtration chromatography of the ultrafiltrate suggested that an endogenous amino thiol-like compound with a molecular weight greater than Mr 1,400 was responsible for the activation. phenolic acid decarboxylase (dpeaa)DE-He213 ferulic acid decarboxylase (dpeaa)DE-He213 -coumaric acid decarboxylase (dpeaa)DE-He213 activator (dpeaa)DE-He213 Chen, Li-Fan verfasserin aut Tokashiki, Masamichi verfasserin aut Ozawa, Tadahiro verfasserin aut Taira, Toki verfasserin aut Ito, Susumu verfasserin aut Enthalten in AMB express Heidelberg : Springer, 2011 2(2012), 1 vom: 04. Jan. (DE-627)665672926 (DE-600)2621432-5 2191-0855 nnns volume:2 year:2012 number:1 day:04 month:01 https://dx.doi.org/10.1186/2191-0855-2-4 lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_SPRINGER SSG-OLC-PHA GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_39 GBV_ILN_40 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_74 GBV_ILN_95 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_161 GBV_ILN_170 GBV_ILN_213 GBV_ILN_230 GBV_ILN_285 GBV_ILN_293 GBV_ILN_602 GBV_ILN_2014 GBV_ILN_4012 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4249 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4700 58.30 ASE AR 2 2012 1 04 01
allfieldsGer	10.1186/2191-0855-2-4 doi (DE-627)SPR031826288 (SPR)2191-0855-2-4-e DE-627 ger DE-627 rakwb eng 570 ASE 58.30 bkl Huang, Hui-Kai verfasserin aut An endogenous factor enhances ferulic acid decarboxylation catalyzed by phenolic acid decarboxylase from Candida guilliermondii 2012 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Abstract The gene for a eukaryotic phenolic acid decarboxylase of Candida guilliermondii was cloned, sequenced, and expressed in Escherichia coli for the first time. The structural gene contained an open reading frame of 504 bp, corresponding to 168 amino acids with a calculated molecular mass of 19,828 Da. The deduced amino sequence exhibited low similarity to those of functional phenolic acid decarboxylases previously reported from bacteria with 25-39% identity and to those of PAD1 and FDC1 proteins from Saccharomyces cerevisiae with less than 14% identity. The C. guilliermondii phenolic acid decarboxylase converted the main substrates ferulic acid and p-coumaric acid to the respective corresponding products. Surprisingly, the ultrafiltrate (Mr 10,000-cut-off) of the cell-free extract of C. guilliermondii remarkably activated the ferulic acid decarboxylation by the purified enzyme, whereas it was almost without effect on the p-coumaric acid decarboxylation. Gel-filtration chromatography of the ultrafiltrate suggested that an endogenous amino thiol-like compound with a molecular weight greater than Mr 1,400 was responsible for the activation. phenolic acid decarboxylase (dpeaa)DE-He213 ferulic acid decarboxylase (dpeaa)DE-He213 -coumaric acid decarboxylase (dpeaa)DE-He213 activator (dpeaa)DE-He213 Chen, Li-Fan verfasserin aut Tokashiki, Masamichi verfasserin aut Ozawa, Tadahiro verfasserin aut Taira, Toki verfasserin aut Ito, Susumu verfasserin aut Enthalten in AMB express Heidelberg : Springer, 2011 2(2012), 1 vom: 04. Jan. (DE-627)665672926 (DE-600)2621432-5 2191-0855 nnns volume:2 year:2012 number:1 day:04 month:01 https://dx.doi.org/10.1186/2191-0855-2-4 lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_SPRINGER SSG-OLC-PHA GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_39 GBV_ILN_40 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_74 GBV_ILN_95 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_161 GBV_ILN_170 GBV_ILN_213 GBV_ILN_230 GBV_ILN_285 GBV_ILN_293 GBV_ILN_602 GBV_ILN_2014 GBV_ILN_4012 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4249 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4700 58.30 ASE AR 2 2012 1 04 01
allfieldsSound	10.1186/2191-0855-2-4 doi (DE-627)SPR031826288 (SPR)2191-0855-2-4-e DE-627 ger DE-627 rakwb eng 570 ASE 58.30 bkl Huang, Hui-Kai verfasserin aut An endogenous factor enhances ferulic acid decarboxylation catalyzed by phenolic acid decarboxylase from Candida guilliermondii 2012 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Abstract The gene for a eukaryotic phenolic acid decarboxylase of Candida guilliermondii was cloned, sequenced, and expressed in Escherichia coli for the first time. The structural gene contained an open reading frame of 504 bp, corresponding to 168 amino acids with a calculated molecular mass of 19,828 Da. The deduced amino sequence exhibited low similarity to those of functional phenolic acid decarboxylases previously reported from bacteria with 25-39% identity and to those of PAD1 and FDC1 proteins from Saccharomyces cerevisiae with less than 14% identity. The C. guilliermondii phenolic acid decarboxylase converted the main substrates ferulic acid and p-coumaric acid to the respective corresponding products. Surprisingly, the ultrafiltrate (Mr 10,000-cut-off) of the cell-free extract of C. guilliermondii remarkably activated the ferulic acid decarboxylation by the purified enzyme, whereas it was almost without effect on the p-coumaric acid decarboxylation. Gel-filtration chromatography of the ultrafiltrate suggested that an endogenous amino thiol-like compound with a molecular weight greater than Mr 1,400 was responsible for the activation. phenolic acid decarboxylase (dpeaa)DE-He213 ferulic acid decarboxylase (dpeaa)DE-He213 -coumaric acid decarboxylase (dpeaa)DE-He213 activator (dpeaa)DE-He213 Chen, Li-Fan verfasserin aut Tokashiki, Masamichi verfasserin aut Ozawa, Tadahiro verfasserin aut Taira, Toki verfasserin aut Ito, Susumu verfasserin aut Enthalten in AMB express Heidelberg : Springer, 2011 2(2012), 1 vom: 04. Jan. (DE-627)665672926 (DE-600)2621432-5 2191-0855 nnns volume:2 year:2012 number:1 day:04 month:01 https://dx.doi.org/10.1186/2191-0855-2-4 lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_SPRINGER SSG-OLC-PHA GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_39 GBV_ILN_40 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_74 GBV_ILN_95 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_161 GBV_ILN_170 GBV_ILN_213 GBV_ILN_230 GBV_ILN_285 GBV_ILN_293 GBV_ILN_602 GBV_ILN_2014 GBV_ILN_4012 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4249 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4700 58.30 ASE AR 2 2012 1 04 01
language	English
source	Enthalten in AMB express 2(2012), 1 vom: 04. Jan. volume:2 year:2012 number:1 day:04 month:01
sourceStr	Enthalten in AMB express 2(2012), 1 vom: 04. Jan. volume:2 year:2012 number:1 day:04 month:01
format_phy_str_mv	Article
institution	findex.gbv.de
topic_facet	phenolic acid decarboxylase ferulic acid decarboxylase -coumaric acid decarboxylase activator
dewey-raw	570
isfreeaccess_bool	false
container_title	AMB express
authorswithroles_txt_mv	Huang, Hui-Kai @@aut@@ Chen, Li-Fan @@aut@@ Tokashiki, Masamichi @@aut@@ Ozawa, Tadahiro @@aut@@ Taira, Toki @@aut@@ Ito, Susumu @@aut@@
publishDateDaySort_date	2012-01-04T00:00:00Z
hierarchy_top_id	665672926
dewey-sort	3570
id	SPR031826288
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author	Huang, Hui-Kai
spellingShingle	Huang, Hui-Kai ddc 570 bkl 58.30 misc phenolic acid decarboxylase misc ferulic acid decarboxylase misc -coumaric acid decarboxylase misc activator An endogenous factor enhances ferulic acid decarboxylation catalyzed by phenolic acid decarboxylase from Candida guilliermondii
authorStr	Huang, Hui-Kai
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topic_title	570 ASE 58.30 bkl An endogenous factor enhances ferulic acid decarboxylation catalyzed by phenolic acid decarboxylase from Candida guilliermondii phenolic acid decarboxylase (dpeaa)DE-He213 ferulic acid decarboxylase (dpeaa)DE-He213 -coumaric acid decarboxylase (dpeaa)DE-He213 activator (dpeaa)DE-He213
topic	ddc 570 bkl 58.30 misc phenolic acid decarboxylase misc ferulic acid decarboxylase misc -coumaric acid decarboxylase misc activator
topic_unstemmed	ddc 570 bkl 58.30 misc phenolic acid decarboxylase misc ferulic acid decarboxylase misc -coumaric acid decarboxylase misc activator
topic_browse	ddc 570 bkl 58.30 misc phenolic acid decarboxylase misc ferulic acid decarboxylase misc -coumaric acid decarboxylase misc activator
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title	An endogenous factor enhances ferulic acid decarboxylation catalyzed by phenolic acid decarboxylase from Candida guilliermondii
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title_full	An endogenous factor enhances ferulic acid decarboxylation catalyzed by phenolic acid decarboxylase from Candida guilliermondii
author_sort	Huang, Hui-Kai
journal	AMB express
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author_browse	Huang, Hui-Kai Chen, Li-Fan Tokashiki, Masamichi Ozawa, Tadahiro Taira, Toki Ito, Susumu
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class	570 ASE 58.30 bkl
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author-letter	Huang, Hui-Kai
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title_sort	endogenous factor enhances ferulic acid decarboxylation catalyzed by phenolic acid decarboxylase from candida guilliermondii
title_auth	An endogenous factor enhances ferulic acid decarboxylation catalyzed by phenolic acid decarboxylase from Candida guilliermondii
abstract	Abstract The gene for a eukaryotic phenolic acid decarboxylase of Candida guilliermondii was cloned, sequenced, and expressed in Escherichia coli for the first time. The structural gene contained an open reading frame of 504 bp, corresponding to 168 amino acids with a calculated molecular mass of 19,828 Da. The deduced amino sequence exhibited low similarity to those of functional phenolic acid decarboxylases previously reported from bacteria with 25-39% identity and to those of PAD1 and FDC1 proteins from Saccharomyces cerevisiae with less than 14% identity. The C. guilliermondii phenolic acid decarboxylase converted the main substrates ferulic acid and p-coumaric acid to the respective corresponding products. Surprisingly, the ultrafiltrate (Mr 10,000-cut-off) of the cell-free extract of C. guilliermondii remarkably activated the ferulic acid decarboxylation by the purified enzyme, whereas it was almost without effect on the p-coumaric acid decarboxylation. Gel-filtration chromatography of the ultrafiltrate suggested that an endogenous amino thiol-like compound with a molecular weight greater than Mr 1,400 was responsible for the activation.
abstractGer	Abstract The gene for a eukaryotic phenolic acid decarboxylase of Candida guilliermondii was cloned, sequenced, and expressed in Escherichia coli for the first time. The structural gene contained an open reading frame of 504 bp, corresponding to 168 amino acids with a calculated molecular mass of 19,828 Da. The deduced amino sequence exhibited low similarity to those of functional phenolic acid decarboxylases previously reported from bacteria with 25-39% identity and to those of PAD1 and FDC1 proteins from Saccharomyces cerevisiae with less than 14% identity. The C. guilliermondii phenolic acid decarboxylase converted the main substrates ferulic acid and p-coumaric acid to the respective corresponding products. Surprisingly, the ultrafiltrate (Mr 10,000-cut-off) of the cell-free extract of C. guilliermondii remarkably activated the ferulic acid decarboxylation by the purified enzyme, whereas it was almost without effect on the p-coumaric acid decarboxylation. Gel-filtration chromatography of the ultrafiltrate suggested that an endogenous amino thiol-like compound with a molecular weight greater than Mr 1,400 was responsible for the activation.
abstract_unstemmed	Abstract The gene for a eukaryotic phenolic acid decarboxylase of Candida guilliermondii was cloned, sequenced, and expressed in Escherichia coli for the first time. The structural gene contained an open reading frame of 504 bp, corresponding to 168 amino acids with a calculated molecular mass of 19,828 Da. The deduced amino sequence exhibited low similarity to those of functional phenolic acid decarboxylases previously reported from bacteria with 25-39% identity and to those of PAD1 and FDC1 proteins from Saccharomyces cerevisiae with less than 14% identity. The C. guilliermondii phenolic acid decarboxylase converted the main substrates ferulic acid and p-coumaric acid to the respective corresponding products. Surprisingly, the ultrafiltrate (Mr 10,000-cut-off) of the cell-free extract of C. guilliermondii remarkably activated the ferulic acid decarboxylation by the purified enzyme, whereas it was almost without effect on the p-coumaric acid decarboxylation. Gel-filtration chromatography of the ultrafiltrate suggested that an endogenous amino thiol-like compound with a molecular weight greater than Mr 1,400 was responsible for the activation.
collection_details	GBV_USEFLAG_A SYSFLAG_A GBV_SPRINGER SSG-OLC-PHA GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_39 GBV_ILN_40 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_74 GBV_ILN_95 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_161 GBV_ILN_170 GBV_ILN_213 GBV_ILN_230 GBV_ILN_285 GBV_ILN_293 GBV_ILN_602 GBV_ILN_2014 GBV_ILN_4012 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4249 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4700
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title_short	An endogenous factor enhances ferulic acid decarboxylation catalyzed by phenolic acid decarboxylase from Candida guilliermondii
url	https://dx.doi.org/10.1186/2191-0855-2-4
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author2	Chen, Li-Fan Tokashiki, Masamichi Ozawa, Tadahiro Taira, Toki Ito, Susumu
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up_date	2024-07-04T01:24:50.611Z
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An endogenous factor enhances ferulic acid decarboxylation catalyzed by phenolic acid decarboxylase from Candida guilliermondii

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