STUDIES ON ATP CITRATE LYASE OF RAT LIVER .V. BINDING SITE OF PHOSPHATE

被引:32
作者
SUZUKI, F
FUKUNISHI, K
TAKEDA, Y
机构
[1] Department of Biochemistry, Osaka University, Osaka
关键词
D O I
10.1093/oxfordjournals.jbchem.a129206
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
The chemical nature of the phosphate bond in the enzyme-P (the enzyme-phosphate complex), the activated intermediate of ATP citrate lyase [EC 4.1.3.8], was investigated. The linkage between the enzyme and phosphate in the complex was more labile in acid than in alkali. The pH stability curve of the enzyme-P is very similar to that of aspartyl phosphate and differs from that of butyl thiophosphate.The phosphorylated form of the enzyme was digested with pronase and the phosphopeptides were isolated by paper electrophoresis. When the phosphopeptides were treated with hydroxylamine, bound phosphates were liberated as P1 with concomitant formation of peptidylhydroxamates. After conversion of the peptidylhydroxamates to the dinitrophenylhydroxamate derivatives, Lossen rearrangement of the latter and the subsequent hydrolysis yieldedα, γ-diaminobutyric acid, indicating the presence of glutamyl-γ-phosphate in the hydroxylamine-sensitive groups of the original protein. From these results, it is concluded that the binding site of phosphate in the phosphorylated intermediate of ATP citrate lyase is the γ-carboxyl groups of glutamic acid residues. © 1969 BY THE JOURNAL OF BIOCHEMISTRY.
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页码:767 / +
页数:1
相关论文
共 28 条
[1]   ISOLATION OF P-32-LABELED PHOSPHOSERINE FROM A YEAST HEXOKINASE PREPARATION, INCUBATED WITH LABELED ATP OR GLUCOSE-6-PHOSPHATE [J].
AGREN, G ;
ENGSTROM, L .
ACTA CHEMICA SCANDINAVICA, 1956, 10 (03) :489-490
[2]   ROLE OF SODIUM IONS IN ACTIVATION OF ELECTROPHORUS ELECTRIC ORGAN ADENOSINE TRIPHOSPHATASE [J].
ALBERS, RW ;
KOVAL, GJ ;
FAHN, S .
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 1963, 50 (03) :474-+
[3]   A STUDY OF THE LINKAGE OF PHOSPHORUS TO PROTEIN IN PHOSPHOGLUCOMUTASE [J].
ANDERSON, L ;
JOLLES, GR .
ARCHIVES OF BIOCHEMISTRY AND BIOPHYSICS, 1957, 70 (01) :121-128
[4]   ISOLATION AND CHARACTERIZATION OF A PHOSPHORYLATED INTERMEDIATE IN (NA+ + K+) SYSTEM-DEPENDENT ATPASE [J].
BADER, H ;
SEN, AK ;
POST, RL .
BIOCHIMICA ET BIOPHYSICA ACTA, 1966, 118 (01) :106-&
[5]  
BLACK S, 1955, J BIOL CHEM, V213, P27
[6]   PARTICIPATION OF ASPARTYL RESIDUES IN HYDROXYLAMINE- OR HYDRAZINE-SENSITIVE BONDS OF COLLAGEN [J].
BLUMENFELD, OO ;
GALLOP, PM .
BIOCHEMISTRY, 1962, 1 (06) :947-+
[7]   EFFECT OF HYDROXYLAMINE AND N-METHYLHYDROXYLAMINE ON BEEF BRAIN MICROSOMAL (NA++K+)-ATPASE [J].
CHIGNELL, CF ;
TITUS, E .
BIOCHIMICA ET BIOPHYSICA ACTA, 1968, 159 (02) :345-&
[8]  
GALLOP PM, 1960, J BIOL CHEM, V235, P2619
[9]   THE MECHANISM OF GLUCOSE-6-PHOSPHATASE [J].
HASS, LF ;
BYRNE, WL .
JOURNAL OF THE AMERICAN CHEMICAL SOCIETY, 1960, 82 (04) :947-954
[10]  
HASS LF, 1961, J BIOL CHEM, V236, P2284