THE ROLE OF CYS-17 IN THE PYRIDOXAL 5'-PHOSPHATE INHIBITION OF THE BOVINE LIVER LOW MR-PHOSPHOTYROSINE PROTEIN PHOSPHATASE

被引：22

作者：

CIRRI, P ^{[1
]}

CHIARUGI, P ^{[1
]}

CAMICI, G ^{[1
]}

MANAO, G ^{[1
]}

PAZZAGLI, L ^{[1
]}

CASELLI, A ^{[1
]}

BARGHINI, I ^{[1
]}

CAPPUGI, G ^{[1
]}

RAUGEI, G ^{[1
]}

RAMPONI, G ^{[1
]}

机构：

[1] UNIV FLORENCE,DIPARTIMENTO SCI BIOCHIM,VIALE MORGAGNI 50,I-50134 FLORENCE,ITALY

来源：

BIOCHIMICA ET BIOPHYSICA ACTA | 1993年 / 1161卷 / 2-3期

关键词：

PHOSPHOTYROSINE PROTEIN PHOSPHATASE; PYRIDOXAL 5'-PHOSPHATE INHIBITION; ACID PHOSPHATASE;

D O I：

10.1016/0167-4838(93)90216-E

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：

Mammalian tissues contain two low M(r) phosphotyrosine protein phosphatase isoforms (type-I and type-2) that differ in the 40-73 amino-acid sequence. Only one isoform (type-2) is strongly inhibited by pyridoxal 5'-phosphate, whereas the other is poorly inhibited by this compound. The mechanism of pyridoxal 5'-phosphate inhibition of the bovine liver enzyme (a type-2 isoform) has been studied by kinetic methods using a series of pyridoxal 5'-phosphate analogues. These studies indicate that pyridoxal 5'-phosphate interacts with the enzyme in both the phosphate and aldehyde groups. Active site-directed mutagenesis has been used to investigate the sites of pyridoxal 5'-phosphate binding. Our results indicate that Cys-17, essential for enzyme activity, interacts with the phosphate moiety of pyridoxal 5'-phosphate. On the other hand, Cys-12, which is also involved in the catalytic mechanism, does not participate in pyridoxal 5'-phosphate binding.

引用

页码：216 / 222

页数：7

共 34 条

[1] RESOLUTION OF THE LOW-MOLECULAR-WEIGHT ACID-PHOSPHATASE IN AVIAN PECTORAL MUSCLE INTO 2 DISTINCT ENZYME FORMS [J].

BAXTER, JH ;

SUELTER, CH .

ARCHIVES OF BIOCHEMISTRY AND BIOPHYSICS, 1985, 239 (01) :29-37

[2]

BENESCH R, 1982, J BIOL CHEM, V257, P1320

[3] THE HUMAN RED-CELL ACID-PHOSPHATASE IS A PHOSPHOTYROSINE PROTEIN PHOSPHATASE WHICH DEPHOSPHORYLATES THE MEMBRANE-PROTEIN BAND-3 [J].

BOIVIN, P ;

GALAND, C .

BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS, 1986, 134 (02) :557-564

[4]

CAMICI G, 1989, J BIOL CHEM, V264, P2560

[5] A MAJOR PHOSPHOTYROSYL-PROTEIN PHOSPHATASE FROM BOVINE HEART IS ASSOCIATED WITH A LOW-MOLECULAR-WEIGHT ACID-PHOSPHATASE [J].

CHERNOFF, J ;

LI, HC .

ARCHIVES OF BIOCHEMISTRY AND BIOPHYSICS, 1985, 240 (01) :135-145

[6]

CHIARUGI P, 1992, IN PRESS FEBS LETT

[7]

DIIANNI CL, 1989, J BIOL CHEM, V264, P8686

[8]

DISSING J, 1991, J BIOL CHEM, V266, P20619

[9] IDENTIFICATION OF THE AMINO-ACID-RESIDUES ESSENTIAL FOR THE ACTIVITY AND THE INTERCONVERSION OF THE MOLECULAR-FORMS OF BILIVERDIN REDUCTASE [J].

FRYDMAN, J ;

TOMARO, ML ;

ROSENFELD, J ;

FRYDMAN, RB .

BIOCHIMICA ET BIOPHYSICA ACTA, 1990, 1040 (01) :119-129

[10]

FUJIMOTO S, 1988, CHEM PHARM BULL, V36, P3020

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