Literature summary for 2.3.1.169 extracted from

Matschiavelli, N.; Oelgeschlaeger, E.; Cocchiararo, B.; Finke, J.; Rother, M.
Function and regulation of isoforms of carbon monoxide dehydrogenase/acetyl coenzyme A synthase in Methanosarcina acetivorans (2012), J. Bacteriol., 194, 5377-5387.

Search for more literature for 2.3.1.169

Cloned(Commentary)

Cloned (Comment)	Organism
two putative operons encoding CODH/ACS, designated cdh1 (ma1016-ma1011) and cdh2 (ma3860-ma3865), both encoding bona fide CODH/ACS isoforms, as well as cdhA3 (ma4399), isogenes organisation, expression of the Cdh2-encoding genes is generally higher than that of genes encoding Cdh1, expression of cdh1, cdh2, and cdhA1 in Escherichia coli	Methanosarcina acetivorans

Protein Variants

Protein Variants	Comment	Organism
additional information	construction of several cdh gene knockouts, genotypic and phenotypic analysis of cdh mutants. CODH activity during aceticlastic and carboxidotrophic growth is reduced in the cdh1 mutant (strain MCD1) compared to the wild-type	Methanosarcina acetivorans

Organism

Organism	UniProt	Comment	Textmining
Methanosarcina acetivorans	-	two CODH/ACS isozymes Cdh1 and Cdh2	-

Source Tissue

Source Tissue	Comment	Organism	Textmining
cell culture	cultures are grown on methanol, acetate, or CO	Methanosarcina acetivorans	-

Synonyms

Synonyms	Comment	Organism
carbon monoxide dehydrogenase/acetyl coenzyme A synthase	-	Methanosarcina acetivorans
CDH1	-	Methanosarcina acetivorans
Cdh2	-	Methanosarcina acetivorans
CO dehydrogenase/acetyl CoA synthase	-	Methanosarcina acetivorans
CO dehydrogenase/acetyl coenzyme A synthase	-	Methanosarcina acetivorans
CODH/ACS	-	Methanosarcina acetivorans

pH Optimum

pH Optimum Minimum	pH Optimum Maximum	Comment	Organism
7.2	-	assay at	Methanosarcina acetivorans

General Information

General Information	Comment	Organism
metabolism	expression of the Cdh1- and Cdh2-encoding genes is regulated differentially in response to growth phase and to changing substrate conditions. CdhA3 clearly affects expression of cdh1, suggesting that it functions in signal perception and transduction rather than in catabolism	Methanosarcina acetivorans
physiological function	the five-subunit archaeal CO dehydrogenase/acetyl CoA synthase multienzyme complex, catalyzing both CO oxidation/CO2 reduction and cleavage/synthesis of acetyl-CoA, is an important enzyme for this process as well as for methanogenic growth on carbon monoxide. Isozyme Cdh1 contributes significantly to overall CODH activity in Methanosarcina acetivorans	Methanosarcina acetivorans

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Release 2023.1 (January 2023)