ELEMENTARY STEPS IN THE REACTION-MECHANISM OF CHICKEN LIVER FATTY-ACID SYNTHASE - REDUCED NICOTINAMIDE ADENINE-DINUCLEOTIDE PHOSPHATE BINDING AND FORMATION AND REDUCTION OF ACETOACETYL-ENZYME

被引：12

作者：

COGNET, JAH ^{[1
]}

COX, BG ^{[1
]}

HAMMES, GG ^{[1
]}

机构：

[1] CORNELL UNIV,DEPT CHEM,ITHACA,NY 14853

来源：

BIOCHEMISTRY | 1983年 / 22卷 / 26期

关键词：

D O I：

10.1021/bi00295a037

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

引用

页码：6281 / 6287

页数：7

共 18 条

[1] ELEMENTARY STEPS IN THE REACTION-MECHANISM OF PYRUVATE-DEHYDROGENASE MULTI-ENZYME COMPLEX FROM ESCHERICHIA-COLI - KINETICS OF FLAVIN REDUCTION
AKIYAMA, SK
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[J]. BIOCHEMISTRY, 1981, 20 (06) : 1491 - 1497
[2] ARSLANIAN MJ, 1976, J BIOL CHEM, V251, P3194
[3] CONTROL MECHANISMS IN SYNTHESIS OF SATURATED FATTY-ACIDS
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VANCE, D
[J]. ANNUAL REVIEW OF BIOCHEMISTRY, 1977, 46 : 263 - 298
[4] INVESTIGATION OF REDUCED NICOTINAMIDE ADENINE-DINUCLEOTIDE PHOSPHATE AND ACYL-BINDING SITES ON AVIAN FATTY-ACID SYNTHASE
CARDON, JW
HAMMES, GG
[J]. BIOCHEMISTRY, 1982, 21 (12) : 2863 - 2870
[5] ELEMENTARY STEPS IN THE REACTION-MECHANISM OF CHICKEN LIVER FATTY-ACID SYNTHASE - ACETYLATION-DEACETYLATION
COGNET, JAH
HAMMES, GG
[J]. BIOCHEMISTRY, 1983, 22 (12) : 3002 - 3007
[6] STEADY-STATE KINETIC-STUDY OF FATTY-ACID SYNTHASE FROM CHICKEN LIVER
COX, BG
HAMMES, GG
[J]. PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA-BIOLOGICAL SCIENCES, 1983, 80 (14): : 4233 - 4237
[7] STABILIZATION AND PHYSICOCHEMICAL PROPERTIES OF FATTY ACID SYNTHETASE OF CHICKEN LIVER
HSU, RY
YUN, SL
[J]. BIOCHEMISTRY, 1970, 9 (02) : 239 - &
[8] REDUCED TRIPHOSPHOPYRIDINE NUCLEOTIDE BINDING SITES OF FATTY ACID SYNTHETASE OF CHICKEN LIVER
HSU, RY
WAGNER, BJ
[J]. BIOCHEMISTRY, 1970, 9 (02) : 245 - &
[9] KATIYAR SS, 1975, J BIOL CHEM, V250, P2709
[10] INACTIVATION OF CHICKEN LIVER FATTY-ACID SYNTHETASE BY MALONYL COENZYME-A - EFFECTS OF ACETYL COENZYME-A AND NICOTINAMIDE ADENINE-DINUCLEOTIDE PHOSPHATE
KUMAR, S
SRINIVASAN, KR
[J]. BIOCHEMISTRY, 1981, 20 (12) : 3393 - 3400

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