J Bacteriol. 1991 Nov;173(21):7029-32.

Purification and partial characterization of 7,8-dihydro-6-hydroxymethylpterin-pyrophosphokinase and 7,8-dihydropteroate synthase from Escherichia coli MC4100.

Talarico TL, Dev IK, Dallas WS, Ferone R, Ray PH.

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Division of Molecular Genetics and Microbiology, Wellcome Research Laboratories, Research Triangle Park, North Carolina 27709.

Abstract

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 greater than 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 greater than 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.

PMID:: 1657875; [PubMed - indexed for MEDLINE]
PMCID:: PMC209061

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Cited by 8 PubMed Central articles

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Structures reported by this article

6-Hydroxymethyl-7,8-Dihydropterin Pyrophosphokinase

PDB: 1HKA

Source: Escherichia coli

Method: X-Ray Diffraction

Resolution: 1.5 Å

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Purification and partial characterization of 7,8-dihydro-6-hydroxymethylpterin-p...
Purification and partial characterization of 7,8-dihydro-6-hydroxymethylpterin-pyrophosphokinase and 7,8-dihydropteroate synthase from Escherichia coli MC4100.
J Bacteriol. 1991 Nov ;173(21):7029-32.

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