Abstract
Menaquinone (vitamin K2)-deficient mutants of Bacillus subtilis, whose growth requirement is satisfied by 1,4-dihydroxy-2-naphthoic acid but not by o-succinylbenzoic acid (OSB), have been analyzed for enzymatic defects. Complementation analysis of cell-free extracts of the mutants revealed that there are two groups, as already indicated by genetic analysis. The missing enzyme in each group was identified by complementation of the cell-free extracts with o-succinylbenzoyl-coenzyme A (CoA) synthetase and dihydroxynaphthoate synthase extracted from Mycobacterium phlei. Mutants found to lack dihydroxynaphthoate synthase, and which therefore complement with dihydroxynaphthoate synthase of M. phlei, were designated as menB; those lacking o-succinylbenzoyl-CoA synthetase, and therefore complementing with o-succinylbenzoyl-CoA synthetase, were designated as menE. The menB mutants RB413 (men-325) and RB415 (men-329), when incubated with [2,3-14C2]OSB, produced only the spirodilactone form of OSB in a reaction that was CoA and adenosine 5'-triphosphate dependent.
Full text
PDF




Selected References
These references are in PubMed. This may not be the complete list of references from this article.
- Bradford M. M. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal Biochem. 1976 May 7;72:248–254. doi: 10.1016/0003-2697(76)90527-3. [DOI] [PubMed] [Google Scholar]
- Bryant R. W., Jr, Bentley R. Menaquinone biosynthesis: conversion of o-succinylbenzoic acid to 1,4-dihydroxy-2-naphthoic acid and menaquinones by Escherichia coli extracts. Biochemistry. 1976 Nov 2;15(22):4792–4796. doi: 10.1021/bi00667a007. [DOI] [PubMed] [Google Scholar]
- Guest J. R. Anaerobic growth of Escherichia coli K12 with fumarate as terminal electron acceptor. Genetic studies with menaquinone and fluoroacetate-resistant mutants. J Gen Microbiol. 1979 Dec;115(2):259–271. doi: 10.1099/00221287-115-2-259. [DOI] [PubMed] [Google Scholar]
- Guest J. R. Menaquinone biosynthesis: mutants of Escherichia coli K-12 requiring 2-succinylbenzoate. J Bacteriol. 1977 Jun;130(3):1038–1046. doi: 10.1128/jb.130.3.1038-1046.1977. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Lambden P. R., Guest J. R. Mutants of Escherichia coli K12 unable to use fumarate as an anaerobic electron acceptor. J Gen Microbiol. 1976 Dec;97(2):145–160. doi: 10.1099/00221287-97-2-145. [DOI] [PubMed] [Google Scholar]
- Meganathan R., Bentley R. Menaquinone (vitamin K2) biosynthesis: conversion of o-succinylbenzoic acid to 1,4-dihydroxy-2-naphthoic acid by Mycobacterium phlei enzymes. J Bacteriol. 1979 Oct;140(1):92–98. doi: 10.1128/jb.140.1.92-98.1979. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Meganathan R., Folger T., Bentley R. Conversion of o-succinylbenzoate to dihydroxynaphthoate by extracts of Micrococcus luteus. Biochemistry. 1980 Feb 19;19(4):785–789. doi: 10.1021/bi00545a026. [DOI] [PubMed] [Google Scholar]
- Săsărman A., Surdeanu M., Portelance V., Dobardzic R., Sonea S. Classification of vitamin K-deficient mutants of Staphylococcus aureus. J Gen Microbiol. 1971 Feb;65(2):125–130. doi: 10.1099/00221287-65-2-125. [DOI] [PubMed] [Google Scholar]
- Taber H. W., Dellers E. A., Lombardo L. R. Menaquinone biosynthesis in Bacillus subtilis: isolation of men mutants and evidence for clustering of men genes. J Bacteriol. 1981 Jan;145(1):321–327. doi: 10.1128/jb.145.1.321-327.1981. [DOI] [PMC free article] [PubMed] [Google Scholar]