Mammalian methylenetetrahydrofolate reductase Partial purification, properties, and inhibition by S-adenosylmethionine
1.5,10-Methylenetetrahydrofolate reductase (5-methyltetrahydrofolate:NAD oxidoreductase, EC 1.1.1.68) has been purified several hundred-fold from both rat and pig liver.2.A spectrophotometric assay for the purified enzyme is given and its optimum conditions have been studied.3.The enzyme is a flavop...
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| Format: |
E-Artikel |
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| Sprache: |
Englisch |
| Erschienen: |
1971 |
|---|
| Reproduktion: |
Elsevier Journal Backfiles on ScienceDirect 1907 - 2002 |
|---|---|
| Übergeordnetes Werk: |
in: BBA - Enzymology - Amsterdam : Elsevier, 250(1971), 3, Seite 459-477 |
| Übergeordnetes Werk: |
volume:250 ; year:1971 ; number:3 ; pages:459-477 |
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| 520 | |a 1.5,10-Methylenetetrahydrofolate reductase (5-methyltetrahydrofolate:NAD oxidoreductase, EC 1.1.1.68) has been purified several hundred-fold from both rat and pig liver.2.A spectrophotometric assay for the purified enzyme is given and its optimum conditions have been studied.3.The enzyme is a flavoprotein specific for FAD.4.The enzyme is specific for NADPH as electron donor and the (+) diastereoisomer of 5,10-CH"2=H"4PteGlu as its physiological substrate. In addition, the enzyme exhibits a strong NADPH-specific diaphorase (reduced-NAD:lipoamide oxidoreductase, EC 1.6.4.3) or menadione reductase (reduced-NAD(P):(acceptor) oxidoreductase, EC 1.6.99.2) activity.5.Apparent K"m values of the pig liver enzyme are: In the reduction of menadione: 49 μM for NADPH, 85 μM for NADH; in the reduction of methylenetetrahydrofolate: 33 μM for NADPH and 310 μM for NADH, and 21 μM for methylenetetrahydrofolate.6.All activities of the enzyme are strongly inhibited by S-adenosylmethionine. This inhibition is partially reversed by S-adenosylhomocysteine. The menadione reductase property of the enzyme is also inhibited by the folate substrates. | ||
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(DE-627)NLEJ185796834 (DE-599)GBVNLZ185796834 DE-627 ger DE-627 rakwb eng Mammalian methylenetetrahydrofolate reductase Partial purification, properties, and inhibition by S-adenosylmethionine 1971 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier 1.5,10-Methylenetetrahydrofolate reductase (5-methyltetrahydrofolate:NAD oxidoreductase, EC 1.1.1.68) has been purified several hundred-fold from both rat and pig liver.2.A spectrophotometric assay for the purified enzyme is given and its optimum conditions have been studied.3.The enzyme is a flavoprotein specific for FAD.4.The enzyme is specific for NADPH as electron donor and the (+) diastereoisomer of 5,10-CH"2=H"4PteGlu as its physiological substrate. In addition, the enzyme exhibits a strong NADPH-specific diaphorase (reduced-NAD:lipoamide oxidoreductase, EC 1.6.4.3) or menadione reductase (reduced-NAD(P):(acceptor) oxidoreductase, EC 1.6.99.2) activity.5.Apparent K"m values of the pig liver enzyme are: In the reduction of menadione: 49 μM for NADPH, 85 μM for NADH; in the reduction of methylenetetrahydrofolate: 33 μM for NADPH and 310 μM for NADH, and 21 μM for methylenetetrahydrofolate.6.All activities of the enzyme are strongly inhibited by S-adenosylmethionine. This inhibition is partially reversed by S-adenosylhomocysteine. The menadione reductase property of the enzyme is also inhibited by the folate substrates. Elsevier Journal Backfiles on ScienceDirect 1907 - 2002 Kutzbach, C. oth Stokstad, E.L.R. oth in BBA - Enzymology Amsterdam : Elsevier 250(1971), 3, Seite 459-477 (DE-627)NLEJ185751202 (DE-600)2209533-0 0005-2744 nnns volume:250 year:1971 number:3 pages:459-477 http://linkinghub.elsevier.com/retrieve/pii/0005-2744(71)90247-6 GBV_USEFLAG_H ZDB-1-SDJ GBV_NL_ARTICLE AR 250 1971 3 459-477 |
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(DE-627)NLEJ185796834 (DE-599)GBVNLZ185796834 DE-627 ger DE-627 rakwb eng Mammalian methylenetetrahydrofolate reductase Partial purification, properties, and inhibition by S-adenosylmethionine 1971 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier 1.5,10-Methylenetetrahydrofolate reductase (5-methyltetrahydrofolate:NAD oxidoreductase, EC 1.1.1.68) has been purified several hundred-fold from both rat and pig liver.2.A spectrophotometric assay for the purified enzyme is given and its optimum conditions have been studied.3.The enzyme is a flavoprotein specific for FAD.4.The enzyme is specific for NADPH as electron donor and the (+) diastereoisomer of 5,10-CH"2=H"4PteGlu as its physiological substrate. In addition, the enzyme exhibits a strong NADPH-specific diaphorase (reduced-NAD:lipoamide oxidoreductase, EC 1.6.4.3) or menadione reductase (reduced-NAD(P):(acceptor) oxidoreductase, EC 1.6.99.2) activity.5.Apparent K"m values of the pig liver enzyme are: In the reduction of menadione: 49 μM for NADPH, 85 μM for NADH; in the reduction of methylenetetrahydrofolate: 33 μM for NADPH and 310 μM for NADH, and 21 μM for methylenetetrahydrofolate.6.All activities of the enzyme are strongly inhibited by S-adenosylmethionine. This inhibition is partially reversed by S-adenosylhomocysteine. The menadione reductase property of the enzyme is also inhibited by the folate substrates. Elsevier Journal Backfiles on ScienceDirect 1907 - 2002 Kutzbach, C. oth Stokstad, E.L.R. oth in BBA - Enzymology Amsterdam : Elsevier 250(1971), 3, Seite 459-477 (DE-627)NLEJ185751202 (DE-600)2209533-0 0005-2744 nnns volume:250 year:1971 number:3 pages:459-477 http://linkinghub.elsevier.com/retrieve/pii/0005-2744(71)90247-6 GBV_USEFLAG_H ZDB-1-SDJ GBV_NL_ARTICLE AR 250 1971 3 459-477 |
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(DE-627)NLEJ185796834 (DE-599)GBVNLZ185796834 DE-627 ger DE-627 rakwb eng Mammalian methylenetetrahydrofolate reductase Partial purification, properties, and inhibition by S-adenosylmethionine 1971 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier 1.5,10-Methylenetetrahydrofolate reductase (5-methyltetrahydrofolate:NAD oxidoreductase, EC 1.1.1.68) has been purified several hundred-fold from both rat and pig liver.2.A spectrophotometric assay for the purified enzyme is given and its optimum conditions have been studied.3.The enzyme is a flavoprotein specific for FAD.4.The enzyme is specific for NADPH as electron donor and the (+) diastereoisomer of 5,10-CH"2=H"4PteGlu as its physiological substrate. In addition, the enzyme exhibits a strong NADPH-specific diaphorase (reduced-NAD:lipoamide oxidoreductase, EC 1.6.4.3) or menadione reductase (reduced-NAD(P):(acceptor) oxidoreductase, EC 1.6.99.2) activity.5.Apparent K"m values of the pig liver enzyme are: In the reduction of menadione: 49 μM for NADPH, 85 μM for NADH; in the reduction of methylenetetrahydrofolate: 33 μM for NADPH and 310 μM for NADH, and 21 μM for methylenetetrahydrofolate.6.All activities of the enzyme are strongly inhibited by S-adenosylmethionine. This inhibition is partially reversed by S-adenosylhomocysteine. The menadione reductase property of the enzyme is also inhibited by the folate substrates. Elsevier Journal Backfiles on ScienceDirect 1907 - 2002 Kutzbach, C. oth Stokstad, E.L.R. oth in BBA - Enzymology Amsterdam : Elsevier 250(1971), 3, Seite 459-477 (DE-627)NLEJ185751202 (DE-600)2209533-0 0005-2744 nnns volume:250 year:1971 number:3 pages:459-477 http://linkinghub.elsevier.com/retrieve/pii/0005-2744(71)90247-6 GBV_USEFLAG_H ZDB-1-SDJ GBV_NL_ARTICLE AR 250 1971 3 459-477 |
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(DE-627)NLEJ185796834 (DE-599)GBVNLZ185796834 DE-627 ger DE-627 rakwb eng Mammalian methylenetetrahydrofolate reductase Partial purification, properties, and inhibition by S-adenosylmethionine 1971 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier 1.5,10-Methylenetetrahydrofolate reductase (5-methyltetrahydrofolate:NAD oxidoreductase, EC 1.1.1.68) has been purified several hundred-fold from both rat and pig liver.2.A spectrophotometric assay for the purified enzyme is given and its optimum conditions have been studied.3.The enzyme is a flavoprotein specific for FAD.4.The enzyme is specific for NADPH as electron donor and the (+) diastereoisomer of 5,10-CH"2=H"4PteGlu as its physiological substrate. In addition, the enzyme exhibits a strong NADPH-specific diaphorase (reduced-NAD:lipoamide oxidoreductase, EC 1.6.4.3) or menadione reductase (reduced-NAD(P):(acceptor) oxidoreductase, EC 1.6.99.2) activity.5.Apparent K"m values of the pig liver enzyme are: In the reduction of menadione: 49 μM for NADPH, 85 μM for NADH; in the reduction of methylenetetrahydrofolate: 33 μM for NADPH and 310 μM for NADH, and 21 μM for methylenetetrahydrofolate.6.All activities of the enzyme are strongly inhibited by S-adenosylmethionine. This inhibition is partially reversed by S-adenosylhomocysteine. The menadione reductase property of the enzyme is also inhibited by the folate substrates. Elsevier Journal Backfiles on ScienceDirect 1907 - 2002 Kutzbach, C. oth Stokstad, E.L.R. oth in BBA - Enzymology Amsterdam : Elsevier 250(1971), 3, Seite 459-477 (DE-627)NLEJ185751202 (DE-600)2209533-0 0005-2744 nnns volume:250 year:1971 number:3 pages:459-477 http://linkinghub.elsevier.com/retrieve/pii/0005-2744(71)90247-6 GBV_USEFLAG_H ZDB-1-SDJ GBV_NL_ARTICLE AR 250 1971 3 459-477 |
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(DE-627)NLEJ185796834 (DE-599)GBVNLZ185796834 DE-627 ger DE-627 rakwb eng Mammalian methylenetetrahydrofolate reductase Partial purification, properties, and inhibition by S-adenosylmethionine 1971 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier 1.5,10-Methylenetetrahydrofolate reductase (5-methyltetrahydrofolate:NAD oxidoreductase, EC 1.1.1.68) has been purified several hundred-fold from both rat and pig liver.2.A spectrophotometric assay for the purified enzyme is given and its optimum conditions have been studied.3.The enzyme is a flavoprotein specific for FAD.4.The enzyme is specific for NADPH as electron donor and the (+) diastereoisomer of 5,10-CH"2=H"4PteGlu as its physiological substrate. In addition, the enzyme exhibits a strong NADPH-specific diaphorase (reduced-NAD:lipoamide oxidoreductase, EC 1.6.4.3) or menadione reductase (reduced-NAD(P):(acceptor) oxidoreductase, EC 1.6.99.2) activity.5.Apparent K"m values of the pig liver enzyme are: In the reduction of menadione: 49 μM for NADPH, 85 μM for NADH; in the reduction of methylenetetrahydrofolate: 33 μM for NADPH and 310 μM for NADH, and 21 μM for methylenetetrahydrofolate.6.All activities of the enzyme are strongly inhibited by S-adenosylmethionine. This inhibition is partially reversed by S-adenosylhomocysteine. The menadione reductase property of the enzyme is also inhibited by the folate substrates. Elsevier Journal Backfiles on ScienceDirect 1907 - 2002 Kutzbach, C. oth Stokstad, E.L.R. oth in BBA - Enzymology Amsterdam : Elsevier 250(1971), 3, Seite 459-477 (DE-627)NLEJ185751202 (DE-600)2209533-0 0005-2744 nnns volume:250 year:1971 number:3 pages:459-477 http://linkinghub.elsevier.com/retrieve/pii/0005-2744(71)90247-6 GBV_USEFLAG_H ZDB-1-SDJ GBV_NL_ARTICLE AR 250 1971 3 459-477 |
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Mammalian methylenetetrahydrofolate reductase Partial purification, properties, and inhibition by S-adenosylmethionine |
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1.5,10-Methylenetetrahydrofolate reductase (5-methyltetrahydrofolate:NAD oxidoreductase, EC 1.1.1.68) has been purified several hundred-fold from both rat and pig liver.2.A spectrophotometric assay for the purified enzyme is given and its optimum conditions have been studied.3.The enzyme is a flavoprotein specific for FAD.4.The enzyme is specific for NADPH as electron donor and the (+) diastereoisomer of 5,10-CH"2=H"4PteGlu as its physiological substrate. In addition, the enzyme exhibits a strong NADPH-specific diaphorase (reduced-NAD:lipoamide oxidoreductase, EC 1.6.4.3) or menadione reductase (reduced-NAD(P):(acceptor) oxidoreductase, EC 1.6.99.2) activity.5.Apparent K"m values of the pig liver enzyme are: In the reduction of menadione: 49 μM for NADPH, 85 μM for NADH; in the reduction of methylenetetrahydrofolate: 33 μM for NADPH and 310 μM for NADH, and 21 μM for methylenetetrahydrofolate.6.All activities of the enzyme are strongly inhibited by S-adenosylmethionine. This inhibition is partially reversed by S-adenosylhomocysteine. The menadione reductase property of the enzyme is also inhibited by the folate substrates. |
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1.5,10-Methylenetetrahydrofolate reductase (5-methyltetrahydrofolate:NAD oxidoreductase, EC 1.1.1.68) has been purified several hundred-fold from both rat and pig liver.2.A spectrophotometric assay for the purified enzyme is given and its optimum conditions have been studied.3.The enzyme is a flavoprotein specific for FAD.4.The enzyme is specific for NADPH as electron donor and the (+) diastereoisomer of 5,10-CH"2=H"4PteGlu as its physiological substrate. In addition, the enzyme exhibits a strong NADPH-specific diaphorase (reduced-NAD:lipoamide oxidoreductase, EC 1.6.4.3) or menadione reductase (reduced-NAD(P):(acceptor) oxidoreductase, EC 1.6.99.2) activity.5.Apparent K"m values of the pig liver enzyme are: In the reduction of menadione: 49 μM for NADPH, 85 μM for NADH; in the reduction of methylenetetrahydrofolate: 33 μM for NADPH and 310 μM for NADH, and 21 μM for methylenetetrahydrofolate.6.All activities of the enzyme are strongly inhibited by S-adenosylmethionine. This inhibition is partially reversed by S-adenosylhomocysteine. The menadione reductase property of the enzyme is also inhibited by the folate substrates. |
| abstract_unstemmed |
1.5,10-Methylenetetrahydrofolate reductase (5-methyltetrahydrofolate:NAD oxidoreductase, EC 1.1.1.68) has been purified several hundred-fold from both rat and pig liver.2.A spectrophotometric assay for the purified enzyme is given and its optimum conditions have been studied.3.The enzyme is a flavoprotein specific for FAD.4.The enzyme is specific for NADPH as electron donor and the (+) diastereoisomer of 5,10-CH"2=H"4PteGlu as its physiological substrate. In addition, the enzyme exhibits a strong NADPH-specific diaphorase (reduced-NAD:lipoamide oxidoreductase, EC 1.6.4.3) or menadione reductase (reduced-NAD(P):(acceptor) oxidoreductase, EC 1.6.99.2) activity.5.Apparent K"m values of the pig liver enzyme are: In the reduction of menadione: 49 μM for NADPH, 85 μM for NADH; in the reduction of methylenetetrahydrofolate: 33 μM for NADPH and 310 μM for NADH, and 21 μM for methylenetetrahydrofolate.6.All activities of the enzyme are strongly inhibited by S-adenosylmethionine. This inhibition is partially reversed by S-adenosylhomocysteine. The menadione reductase property of the enzyme is also inhibited by the folate substrates. |
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<?xml version="1.0" encoding="UTF-8"?><collection xmlns="http://www.loc.gov/MARC21/slim"><record><leader>01000caa a22002652 4500</leader><controlfield tag="001">NLEJ185796834</controlfield><controlfield tag="003">DE-627</controlfield><controlfield tag="005">20210707025457.0</controlfield><controlfield tag="007">cr uuu---uuuuu</controlfield><controlfield tag="008">070506s1971 xx |||||o 00| ||eng c</controlfield><datafield tag="035" ind1=" " ind2=" "><subfield code="a">(DE-627)NLEJ185796834</subfield></datafield><datafield tag="035" ind1=" " ind2=" "><subfield code="a">(DE-599)GBVNLZ185796834</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="245" ind1="1" ind2="0"><subfield code="a">Mammalian methylenetetrahydrofolate reductase Partial purification, properties, and inhibition by S-adenosylmethionine</subfield></datafield><datafield tag="264" ind1=" " ind2="1"><subfield code="c">1971</subfield></datafield><datafield tag="336" ind1=" " ind2=" "><subfield code="a">nicht spezifiziert</subfield><subfield code="b">zzz</subfield><subfield code="2">rdacontent</subfield></datafield><datafield tag="337" ind1=" " ind2=" "><subfield code="a">nicht spezifiziert</subfield><subfield code="b">z</subfield><subfield code="2">rdamedia</subfield></datafield><datafield tag="338" ind1=" " ind2=" "><subfield code="a">nicht spezifiziert</subfield><subfield code="b">zu</subfield><subfield code="2">rdacarrier</subfield></datafield><datafield tag="520" ind1=" " ind2=" "><subfield code="a">1.5,10-Methylenetetrahydrofolate reductase (5-methyltetrahydrofolate:NAD oxidoreductase, EC 1.1.1.68) has been purified several hundred-fold from both rat and pig liver.2.A spectrophotometric assay for the purified enzyme is given and its optimum conditions have been studied.3.The enzyme is a flavoprotein specific for FAD.4.The enzyme is specific for NADPH as electron donor and the (+) diastereoisomer of 5,10-CH"2=H"4PteGlu as its physiological substrate. In addition, the enzyme exhibits a strong NADPH-specific diaphorase (reduced-NAD:lipoamide oxidoreductase, EC 1.6.4.3) or menadione reductase (reduced-NAD(P):(acceptor) oxidoreductase, EC 1.6.99.2) activity.5.Apparent K"m values of the pig liver enzyme are: In the reduction of menadione: 49 μM for NADPH, 85 μM for NADH; in the reduction of methylenetetrahydrofolate: 33 μM for NADPH and 310 μM for NADH, and 21 μM for methylenetetrahydrofolate.6.All activities of the enzyme are strongly inhibited by S-adenosylmethionine. This inhibition is partially reversed by S-adenosylhomocysteine. The menadione reductase property of the enzyme is also inhibited by the folate substrates.</subfield></datafield><datafield tag="533" ind1=" " ind2=" "><subfield code="f">Elsevier Journal Backfiles on ScienceDirect 1907 - 2002</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Kutzbach, C.</subfield><subfield code="4">oth</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Stokstad, E.L.R.</subfield><subfield code="4">oth</subfield></datafield><datafield tag="773" ind1="0" ind2="8"><subfield code="i">in</subfield><subfield code="t">BBA - Enzymology</subfield><subfield code="d">Amsterdam : Elsevier</subfield><subfield code="g">250(1971), 3, Seite 459-477</subfield><subfield code="w">(DE-627)NLEJ185751202</subfield><subfield code="w">(DE-600)2209533-0</subfield><subfield code="x">0005-2744</subfield><subfield code="7">nnns</subfield></datafield><datafield tag="773" ind1="1" ind2="8"><subfield code="g">volume:250</subfield><subfield code="g">year:1971</subfield><subfield code="g">number:3</subfield><subfield code="g">pages:459-477</subfield></datafield><datafield tag="856" ind1="4" ind2="0"><subfield code="u">http://linkinghub.elsevier.com/retrieve/pii/0005-2744(71)90247-6</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_USEFLAG_H</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">ZDB-1-SDJ</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_NL_ARTICLE</subfield></datafield><datafield tag="951" ind1=" " ind2=" "><subfield code="a">AR</subfield></datafield><datafield tag="952" ind1=" " ind2=" "><subfield code="d">250</subfield><subfield code="j">1971</subfield><subfield code="e">3</subfield><subfield code="h">459-477</subfield></datafield></record></collection>
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