STEADY-STATE KINETICS AND INHIBITION STUDIES OF THE ALDOL CONDENSATION REACTION CATALYZED BY BOVINE LIVER AND ESCHERICHIA-COLI 2-KETO-4-HYDROXYGLUTARATE ALDOLASE

被引：9

作者：

GRADY, SR ^{[1
]}

WANG, JK ^{[1
]}

DEKKER, EE ^{[1
]}

机构：

[1] UNIV MICHIGAN,DEPT BIOL CHEM,ANN ARBOR,MI 48109

来源：

BIOCHEMISTRY | 1981年 / 20卷 / 09期

关键词：

D O I：

10.1021/bi00512a021

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：2497 / 2502

页数：6

共 41 条

[21] AMINO-ACID-SEQUENCE OF THE PYRUVATE AND THE GLYOXYLATE ACTIVE-SITE LYSINE PEPTIDE OF ESCHERICHIA-COLI 2-KETO-4-HYDROXYGLUTARATE ALDOLASE
VLAHOS, CJ
DEKKER, EE
JOURNAL OF BIOLOGICAL CHEMISTRY, 1986, 261 (24) : 1049 - 1055
[22] PURIFICATION, SUBSTRATE-SPECIFICITY AND BINDING, BETA-DECARBOXYLASE ACTIVITY, AND OTHER PROPERTIES OF ESCHERICHIA-COLI 2-KETO-4-HYDROXYGLUTARATE ALDOLASE
NISHIHARA, H
DEKKER, EE
JOURNAL OF BIOLOGICAL CHEMISTRY, 1972, 247 (16) : 5079 - +
[23] ACTIVE-SITE RESIDUES OF 2-KETO-4-HYDROXYGLUTARATE ALDOLASE FROM ESCHERICHIA-COLI - BROMOPYRUVATE INACTIVATION AND LABELING OF GLUTAMATE-45
VLAHOS, CJ
DEKKER, EE
JOURNAL OF BIOLOGICAL CHEMISTRY, 1990, 265 (33) : 20384 - 20389
[24] EVIDENCE FOR AN ESSENTIAL ARGININE RESIDUE IN THE ACTIVE-SITE OF ESCHERICHIA-COLI 2-KETO-4-HYDROXYGLUTARATE ALDOLASE - MODIFICATION WITH 1,2-CYCLOHEXANEDIONE
VLAHOS, CJ
GHALAMBOR, MA
DEKKER, EE
JOURNAL OF BIOLOGICAL CHEMISTRY, 1985, 260 (09) : 5480 - 5485
[25] AMINO-ACID SEQUENCE OF THE PYRUVATE AND THE GLYOXYLATE ACTIVE-SITE LYSINE PEPTIDE OF ESCHERICHIA-COLI 2-KETO-4-HYDROXYGLUTARATE (KHG) ALDOLASE
VLAHOS, CJ
DEKKER, EE
FEDERATION PROCEEDINGS, 1985, 44 (04) : 1059 - 1059
[26] OXIDATION OF 2-KETO-4-HYDROXYGLUTARATE BY PIG HEART AND ESCHERICHIA-COLI ALPHA-KETOGLUTARATE DEHYDROGENASE COMPLEX
GUPTA, SC
DEKKER, EE
ARCHIVES OF BIOCHEMISTRY AND BIOPHYSICS, 1979, 192 (01) : 324 - 326
[27] LIPOAMIDE DEHYDROGENASE FROM ESCHERICHIA-COLI - STEADY-STATE KINETICS OF THE PHYSIOLOGICAL REACTION
SAHLMAN, L
WILLIAMS, CH
JOURNAL OF BIOLOGICAL CHEMISTRY, 1989, 264 (14) : 8039 - 8045
[28] BROMOPYRUVATE, AN ACTIVE SITE-DIRECTED INACTIVATOR OF ESCHERICHIA-COLI 2-KETO-4-HYDROXYGLUTARATE(KHG) ALDOLASE, MODIFIES GLUTAMIC-ACID RESIDUE-45
VLAHOS, CJ
DEKKER, EE
FEDERATION PROCEEDINGS, 1987, 46 (06) : 2167 - 2167
[29] SITE-DIRECTED MUTAGENESIS OF 2-KETO-4-HYDROXYGLUTARATE (KHG) ALDOLASE FROM ESCHERICHIA-COLI SUPPORTS THE ROLE OF GLU-45 AS AN AMPHOTERIC PROTON DONOR/ACCEPTOR
PATIL, RV
DEKKER, EE
FASEB JOURNAL, 1991, 5 (04): : A826 - A826
[30] Sugar recognition by the glucose and mannose permeases of Escherichia coli.: Steady-state kinetics and inhibition studies
García-Alles, LF
Zahn, A
Erni, B
BIOCHEMISTRY, 2002, 41 (31) : 10077 - 10086

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