Abstract:
:In Clostridium thermoaceticum, the synthesis of acetyl-CoA from methyl tetrahydrofolate occurs via a series of enzymatic reactions involving methyl transferase, corrinoid/Fe-S protein (corrinoid), carbon monoxide dehydrogenase (CODH) and ferredoxin. We have investigated the possibility of one or more of these proteins existing as multi-enzyme complexes in vivo with higher catalytic activity. A protein complex consisting of CODH and corrinoid was isolated from the cell-free extracts of Clostridium thermoaceticum. The acetyl-CoA synthesis was found to be approximately 1.8-fold higher with the complex than that observed with the isolated protein components. HPLC gel filtration analyses of the native and DTE reduced complex suggested that the CODH:corrinoid complex is held together primarily by an inter disulfide bond. By differential labeling of thiols with [14C]N-ethylmaleimide it was found that Cys-506 of the alpha subunit of CODH was involved in the disulfide linkage with the corrinoid of the complex.
journal_name
FEBS Lettjournal_title
FEBS lettersauthors
Shanmugasundaram T,Sundaresh CS,Kumar GKdoi
10.1016/0014-5793(93)81808-dsubject
Has Abstractpub_date
1993-07-12 00:00:00pages
281-4issue
1-3eissn
0014-5793issn
1873-3468pii
0014-5793(93)81808-Djournal_volume
326pub_type
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