Abstract:
:The committed step in menaquinone biosynthesis is the formation of o-succinylbenzoate (OSB). It is presumed to require the reaction of a seven-carbon intermediate of the shikimate pathway with a succinic semialdehyde-thiamin pyrophosphate (TPP) anion, derived by decarboxylation of 2-ketoglutarate. The following evidence indicates that the decarboxylation is not a function of the ketoglutarate dehydrogenase complex but is carried out by a separate activity. (A) Cell-free extracts of Escherichia coli K12 without added TPP lose OSB synthase activity but retain all of the ketoglutarate dehydrogenase complex activities. (B) OSB synthase activity is inhibited by addition of tetrahydro-TPP (th-TPP) to the incubations. The ketoglutarate dehydrogenase complex activities are only inhibited by this analogue after an initial preincubation period. (C) The high molecular weight ketoglutarate dehydrogenase complex can be separated from OSB synthase activity by gel-permeation chromatography on Sepharose CL-6B. Experiment series A and B also provide supporting evidence that TPP does play an important role in menaquinone biosynthesis.
journal_name
Biochemistryjournal_title
Biochemistryauthors
Marley MG,Meganathan R,Bentley Rdoi
10.1021/bi00354a017subject
Has Abstractpub_date
1986-03-25 00:00:00pages
1304-7issue
6eissn
0006-2960issn
1520-4995journal_volume
25pub_type
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