Acetyl-CoA decarbonylase/synthase complex from Archaeoglobus fulgidus

The acetyl-CoA decarbonylase/synthase (ACDS) multienzyme complex catalyzes the reversible cleavage and synthesis of acetyl-CoA in methanogens. This report of the enzyme complex in Archaeoglobus fulgidus demonstrates the existence of a functional ACDS complex in an organism that is not a methanogen....

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Bibliographic Details
Published in:	Archives of microbiology Vol. 169; no. 6; pp. 525 - 529
Main Authors:	DAI, Y.-R, REED, D. W, MILLSTEIN, J. H, HARTZELL, P. L, GRAHAME, D. A, DEMOLL, E
Format:	Journal Article
Language:	English
Published:	Heidelberg Springer 01-06-1998 Berlin
Subjects:	Aldehyde Oxidoreductases - chemistry Aldehyde Oxidoreductases - isolation & purification Aldehyde Oxidoreductases - metabolism Amino Acid Sequence Archaeal Proteins - chemistry Archaeal Proteins - isolation & purification Archaeal Proteins - metabolism Archaeoglobus fulgidus - enzymology Bacteriology Biological and medical sciences Blotting, Western Electrophoresis, Polyacrylamide Gel Fundamental and applied biological sciences. Psychology Metabolism. Enzymes Microbiology Molecular Sequence Data Multienzyme Complexes - chemistry Multienzyme Complexes - isolation & purification Multienzyme Complexes - metabolism Characterization Purification Multienzyme complex Archaeobacteria Enzyme Bacteria Acetyl coenzyme A Metabolism Structural analysis
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Summary:	The acetyl-CoA decarbonylase/synthase (ACDS) multienzyme complex catalyzes the reversible cleavage and synthesis of acetyl-CoA in methanogens. This report of the enzyme complex in Archaeoglobus fulgidus demonstrates the existence of a functional ACDS complex in an organism that is not a methanogen. The A. fulgidus enzyme complex contained five subunits of 89, 72, 50, 49.5, and 18.5 kDa, and it catalyzed the overall synthesis of acetyl-CoA according to the following reaction: CO2 + 2 Fdred(Fe2+) + 2 H+ + CH3 - H4SPt + CoA <==> acetyl-CoA + H4SPt + 2 Fdox(Fe3+) + H2O where Fd is ferredoxin, and CH3-H4SPt and H4SPt denote N5-methyl-tetrahydrosarcinapterin and tetrahydrosarcinapterin, respectively.
Bibliography:	ObjectType-Article-2 SourceType-Scholarly Journals-1 ObjectType-Feature-1 content type line 23 ObjectType-Article-1 ObjectType-Feature-2
ISSN:	0302-8933 1432-072X
DOI:	10.1007/s002030050606