Biochemical evidence that Escherichia coli hyi (orf b0508, gip) gene encodes hydroxypyruvate isomerase

被引：23

作者：

Ashiuchi, M ^{[1
]}

Misono, H ^{[1
]}

机构：

[1] Kochi Univ, Fac Agr, Dept Bioresource Sci, Nankoku, Kochi 7838502, Japan

来源：

BIOCHIMICA ET BIOPHYSICA ACTA-PROTEIN STRUCTURE AND MOLECULAR ENZYMOLOGY | 1999年 / 1435卷 / 1-2期

关键词：

hydroxypyruvate isomerase; glyoxylate-induced protein; overproduction; purification; Escherichia coli;

D O I：

10.1016/S0167-4838(99)00216-2

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：

We found a significant activity of hydroxypyruvate isomerase in Escherichia coli clone cells harboring an E. coli gene (called orf b0508 or gip), which is located downstream of the glyoxylate carboligase gene. We newly designated the gene hyi. The enzyme was purified from cell extracts of the E. coli clone. The enzyme had a molecular mass of 58 kDa and was composed of two identical subunits. The optimum pH for the isomerization of hydroxypyruvate was 6.8-7.2. The enzyme required no cofactor. It exclusively catalyzed the isomerization between hydroxypyruvate and tartronate semialdehyde. The apparent K-m value for hydroxypyruvate was 12.5 mM. The amino acid sequence of E. coli hydroxypyruvate isomerase is highly similar to those of glyoxylate-induced proteins, Gip, found widely from prokaryotes to eukaryotes. (C) 1999 Elsevier Science B.V. All rights reserved.

引用

页码：153 / 159

页数：7

共 24 条

[1]

Ashiuchi M, 1998, J BIOCHEM-TOKYO, V123, P1156

[2] Escherichia coli diacylglycerol kinase is an evolutionarily optimized membrane enzyme and catalyzes direct phosphoryl transfer [J].

Badola, P ;

Sanders, CR .

JOURNAL OF BIOLOGICAL CHEMISTRY, 1997, 272 (39) :24176-24182

[3] The complete genome sequence of Escherichia coli K-12 [J].

Blattner, FR ;

Plunkett, G ;

Bloch, CA ;

Perna, NT ;

Burland, V ;

Riley, M ;

ColladoVides, J ;

Glasner, JD ;

Rode, CK ;

Mayhew, GF ;

Gregor, J ;

Davis, NW ;

Kirkpatrick, HA ;

Goeden, MA ;

Rose, DJ ;

Mau, B ;

Shao, Y .

SCIENCE, 1997, 277 (5331) :1453-+

[4]

CHANG YY, 1993, J BIOL CHEM, V268, P3911

[5] PURIFICATION AND SOME PROPERTIES OF HYDROXYPYRUVATE ISOMERASE OF BACILLUS-FASTIDIOSUS [J].

DEWINDT, FE ;

VANDERDRIFT, C .

BIOCHIMICA ET BIOPHYSICA ACTA, 1980, 613 (02) :556-562

[6] IDENTIFICATION OF THE ESCHERICHIA-COLI MURI GENE, WHICH IS REQUIRED FOR THE BIOSYNTHESIS OF D-GLUTAMIC ACID, A SPECIFIC COMPONENT OF BACTERIAL PEPTIDOGLYCAN [J].

DOUBLET, P ;

VANHEIJENOORT, J ;

MENGINLECREULX, D .

JOURNAL OF BACTERIOLOGY, 1992, 174 (18) :5772-5779

[7] WHOLE-GENOME RANDOM SEQUENCING AND ASSEMBLY OF HAEMOPHILUS-INFLUENZAE RD [J].

FLEISCHMANN, RD ;

ADAMS, MD ;

WHITE, O ;

CLAYTON, RA ;

KIRKNESS, EF ;

KERLAVAGE, AR ;

BULT, CJ ;

TOMB, JF ;

DOUGHERTY, BA ;

MERRICK, JM ;

MCKENNEY, K ;

SUTTON, G ;

FITZHUGH, W ;

FIELDS, C ;

GOCAYNE, JD ;

SCOTT, J ;

SHIRLEY, R ;

LIU, LI ;

GLODEK, A ;

KELLEY, JM ;

WEIDMAN, JF ;

PHILLIPS, CA ;

SPRIGGS, T ;

HEDBLOM, E ;

COTTON, MD ;

UTTERBACK, TR ;

HANNA, MC ;

NGUYEN, DT ;

SAUDEK, DM ;

BRANDON, RC ;

FINE, LD ;

FRITCHMAN, JL ;

FUHRMANN, JL ;

GEOGHAGEN, NSM ;

GNEHM, CL ;

MCDONALD, LA ;

SMALL, KV ;

FRASER, CM ;

SMITH, HO ;

VENTER, JC .

SCIENCE, 1995, 269 (5223) :496-512

[8]

HEDRICK JL, 1961, J BIOL CHEM, V236, P1867

[9] UDP-N-ACETYLMURAMYL-L-ALANINE FUNCTIONS AS AN ACTIVATOR IN THE REGULATION OF THE ESCHERICHIA-COLI GLUTAMATE RACEMASE ACTIVITY [J].

HO, HT ;

FALK, PJ ;

ERVIN, KM ;

KRISHNAN, BS ;

DISCOTTO, LF ;

DOUGHERTY, TJ ;

PUCCI, MJ .

BIOCHEMISTRY, 1995, 34 (08) :2464-2470

[10] Evolution of enzymatic activities in the enolase superfamily:: Characterization of the (D)-glucarate/galactarate catabolic pathway in Escherichia coli [J].

Hubbard, BK ;

Koch, M ;

Palmer, DRJ ;

Babbitt, PC ;

Gerlt, JA .

BIOCHEMISTRY, 1998, 37 (41) :14369-14375

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