PURIFICATION AND PARTIAL CHARACTERIZATION OF 7,8-DIHYDRO-6-HYDROXYMETHYLPTERIN-PYROPHOSPHOKINASE AND 7,8-DIHYDROPTEROATE SYNTHASE FROM ESCHERICHIA-COLI MC4100

被引：30

作者：

TALARICO, TL ^{[1
]}

DEV, IK ^{[1
]}

DALLAS, WS ^{[1
]}

FERONE, R ^{[1
]}

RAY, PH ^{[1
]}

机构：

[1] WELLCOME RES LABS,DIV MOLEC GENET & MICROBIOL,RES TRIANGLE PK,NC 27709

来源：

JOURNAL OF BACTERIOLOGY | 1991年 / 173卷 / 21期

关键词：

D O I：

10.1128/jb.173.21.7029-7032.1991

中图分类号：

Q93 [微生物学];

学科分类号：

071005 ; 100705 ;

摘要：

The enzymes 7,8-dihydroxymethylpterin-pyrophosphokinase (HPPK) and 7,8-dihydropteroate synthase (DHPS), which act sequentially in the folate pathway, were purified to homogeneity from crude extracts of Escherichia coli MC4100. The enzymes represent less than 0.01% of the total soluble protein. HPPK was purified > 10,000-fold; the native enzyme appears to be a monomer with a molecular mass of 25 kDa and a pI of 5.2. DHPS was purified > 7,000-fold; the native enzyme has an apparent molecular mass of 52 to 54 kDa and is composed of two identical 30-kDa subunits. The amino-terminal sequences for both enzymes have been determined.

引用

页码：7029 / 7032

页数：4

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