GLUTACONATE COA-TRANSFERASE FROM ACIDAMINOCOCCUS-FERMENTANS
GLUTACONATE COA-TRANSFERASE FROM ACIDAMINOCOCCUS-FERMENTANS
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DOI:
10.1111/j.1432-1033.1981.tb06404.x
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发表时间:
1981-01-01
期刊:
影响因子:
--
通讯作者:
SEMMLER, R
中科院分区:
文献类型:
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作者:
BUCKEL, W;DORN, U;SEMMLER, R
A. fermentans glutaconate CoA-transferase catalyzes the transfer of CoAS- from acetyl-CoA preferentially to (E)-glutaconate, but glutarate, (R)-2-hydroxyglutarate, acrylate and propionate are also good acceptors. No reaction was observed with (Z)-glutaconate and C4-dicarboxylic acids. The product of the reaction of acetyl-CoA with (E)-glutaconate is the 1-isomer of glutaconyl-CoA, i.e., the thiol ester is conjugated with the double bond. With (R)-2-hydroxyglutarate as substrate, both possible isomers are generated. Glutaconate CoA-transferase was purified from cell-free extracts of A. fermentans to apparent homogeneity and crystallized. The relative molecular mass of the enzyme is .apprx. 275,000. It consists of 2 different polypeptide chains (MW 32,000 and 34,000). On the catalytic pathway a thiolester is formed between CoASH and a carboxylate of the smaller polypeptide chain. The structural and functional relationships between glutaconate CoA-transferase and other CoA-transferases are discussed. Glutaconate CoA-transferase is also present in other bacteria fermenting glutamate via hydroxyglutarate. Experiments with an antiserum against the enzyme indicate that the transferase is necessary for the decarboxylation of glutaconate but not for the dehydration of (R)-2-hydroxyglutarate.