ISOLATION AND CHARACTERIZATION OF THE THERMORESISTANT GLUCONOKINASE FROM ESCHERICHIA-COLI

被引：2

作者：

VIVAS, EI

LIENDO, A

DAWIDOWICZ, K

ISTURIZ, T

机构：

[1] CENT UNIV VENEZUELA,FAC CIENCIAS,ESCUELA BIOL,CTR BIOL CELULAR,CARACAS 1041A,VENEZUELA

[2] CENT UNIV VENEZUELA,FAC CIENCIAS,ESCUELA BIOL,DEPT BIOL CELULAR,CARACAS 1041A,VENEZUELA

来源：

JOURNAL OF BASIC MICROBIOLOGY | 1994年 / 34卷 / 02期

关键词：

D O I：

10.1002/jobm.3620340207

中图分类号：

Q93 [微生物学];

学科分类号：

071005 ; 100705 ;

摘要：

It is known that two gluconokinases are inducibly expressed during the utilization of gluconate by E. coli. One is thermoresistant (activity stable for 3 h at 30 degrees C) and the other thermosensitive (losses 75% or more of its activity under the above conditions). The thermoresistant gluconokinase (EC 2.7.1.12) was isolated, purified and characterized for the first time from the E. coli mutant Ca26, a K12 derivative which lacks the thermosensitive activity. The enzyme was purified 43 fold with a recovery of 11%. The M(r) of the enzyme was 100 kDa with three equal subunits of approximately 29.5 kDa. The enzyme exhibited MICHAELIS-MENTEN kinetics and the K-m values for gluconate and ATP were 0.02 mM and 0.045 mM respectively.

引用

页码：117 / 122

页数：6

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