ELEMENTARY STEPS IN THE REACTION-MECHANISM OF THE ALPHA-KETOGLUTARATE DEHYDROGENASE MULTIENZYME COMPLEX FROM ESCHERICHIA-COLI - KINETICS OF SUCCINYLATION AND DESUCCINYLATION

被引：24

作者：

WASKIEWICZ, DE ^{[1
]}

HAMMES, GG ^{[1
]}

机构：

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

来源：

BIOCHEMISTRY | 1984年 / 23卷 / 14期

关键词：

D O I：

10.1021/bi00309a005

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：3136 / 3143

页数：8

共 49 条

[41] INHIBITION OF PYRUVATE-DEHYDROGENASE MULTIENZYME COMPLEX FROM ESCHERICHIA-COLI WITH A RADIOLABELED BIFUNCTIONAL ARSENOXIDE - EVIDENCE FOR AN ESSENTIAL HISTIDINE RESIDUE AT THE ACTIVE-SITE OF LIPOAMIDE DEHYDROGENASE
ADAMSON, SR
ROBINSON, JA
STEVENSON, KJ
BIOCHEMISTRY, 1984, 23 (06) : 1269 - 1274
[42] REACTION-MECHANISM OF RIBONUCLEOSIDE DIPHOSPHATE REDUCTASE FROM ESCHERICHIA-COLI - OXIDATION-REDUCTION ACTIVE DISULFIDES IN B1 SUBUNIT
THELANDER, L
JOURNAL OF BIOLOGICAL CHEMISTRY, 1974, 249 (15) : 4858 - 4862
[43] THE CATALYTIC MECHANISM OF TRYPTOPHAN SYNTHASE FROM ESCHERICHIA-COLI - KINETICS OF THE REACTION OF INDOLE WITH THE ENZYME-L-SERINE COMPLEXES
LANE, AN
KIRSCHNER, K
EUROPEAN JOURNAL OF BIOCHEMISTRY, 1983, 129 (03): : 571 - 582
[44] 3-DIMENSIONAL SOLUTION STRUCTURE OF THE E3-BINDING DOMAIN OF THE DIHYDROLIPOAMIDE SUCCINYL TRANSFERASE CORE FROM THE 2-OXOGLUTARATE DEHYDROGENASE MULTIENZYME COMPLEX OF ESCHERICHIA-COLI
ROBIEN, MA
CLORE, GM
OMICHINSKI, JG
PERHAM, RN
APPELLA, E
SAKAGUCHI, K
GRONENBORN, AM
BIOCHEMISTRY, 1992, 31 (13) : 3463 - 3471
[45] EPIMERIZATION OF 3-HYDROXY-4-TRANS-DECENOYL COENZYME-A BY A DEHYDRATION HYDRATION MECHANISM CATALYZED BY THE MULTIENZYME COMPLEX OF FATTY-ACID OXIDATION FROM ESCHERICHIA-COLI
SMELAND, TE
CUEBAS, D
SCHULZ, H
JOURNAL OF BIOLOGICAL CHEMISTRY, 1991, 266 (35) : 23904 - 23908
[46] KINETICS OF OPEN COMPLEX-FORMATION BETWEEN ESCHERICHIA-COLI RNA-POLYMERASE AND THE LAC UV5 PROMOTER - EVIDENCE FOR A SEQUENTIAL MECHANISM INVOLVING 3 STEPS
BUC, H
MCCLURE, WR
BIOCHEMISTRY, 1985, 24 (11) : 2712 - 2723
[47] Histidine-450 is the catalytic residue of L-3-hydroxyacyl coenzyme a dehydrogenase associated with the large alpha-subunit of the multienzyme complex of fatty acid oxidation from Escherichia coli
He, XY
Yang, SY
BIOCHEMISTRY, 1996, 35 (29) : 9625 - 9630
[48] STUDIES ON REACTION-MECHANISM OF ADENOSINE-TRIPHOSPHATE - GLUTAMINE SYNTHETASE ADENYLYLTRANSFERASE FROM ESCHERICHIA-COLI B - CONFORMATIONAL-CHANGES ELICITED BY EFFECTORS AND SUBSTRATES - REACTIVITY OF SULFHYDRYL GROUPS
WOLF, DH
EBNER, E
JOURNAL OF BIOLOGICAL CHEMISTRY, 1972, 247 (13) : 4208 - &
[49] GLUTAMATE 139 OF THE LARGE ALPHA-SUBUNIT IS THE CATALYTIC BASE IN THE DEHYDRATION OF BOTH D-3-HYDROXYACYL-COENZYME AND L-3-HYDROXYACYL-COENZYME A BUT NOT IN THE ISOMERIZATION OF DELTA(3),DELTA(2)-ENOYL-COENZYME-A CATALYZED BY THE MULTIENZYME COMPLEX OF FATTY-ACID OXIDATION FROM ESCHERICHIA-COLI
YANG, SY
HE, XY
SCHULZ, H
BIOCHEMISTRY, 1995, 34 (19) : 6441 - 6447

← 1 2 3 4 5 →