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Query: UMLS:C0027960 (mole)
 21,279 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The purpose of the present study was to determine if the enoyl coenzyme A hydratase formed by Pseudomonas putida during growth on isoleucine was a unique enzyme specific for isoleucine metabolism. The highest levels of the hydratase were formed during growth on isoleucine intermediates and the lowest levels during growth on glutamate and glucose. Data from growth experiments revealed that 2-methyl-3-hydroxybutyryl coenzyme A hydratase, an enzyme unique to isoleucine metabolism and enoyl coenzyme A hydratase were coordinately induced, but that 3-hydroxyacyl coenzyme A dehydrogenase was under separate control. The hydratase was purified 180-fold from isoleucine cells, and its physical and catalytic properties reported. The highest activity was with crotonyl coenzyme A,Vmax = 1100 x 10(3) moles/min mole enzyme, next was tiglyl coenzyme A, Vmax = 61 x 10(3) moles/min mole enzyme, and last was 3-methyl-crotonyl coenzyme A, Vmax = 2.3 x 10(3) moles/min mole enzyme. Enzyme purified from butyrate cells had the same elution patterns during column chromatography and catalytic properties as the enzyme from isoleucine cells. These data support the conclusion that a single enzyme in P. putida is responsible for the hydration of both tiglyl coenzyme A and crotonyl coenzyme A.
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PMID:The role of enoyl-coa hydratase in the metabolism of isoleucine by Pseudomonas putida. 67 16

Freeze-thawed rat liver mitochondria were extensively washed with potassium phosphate, pH 7.5, and the residue was extracted with 10 mM potassium phosphate, pH 7.5, 1% (w/v) sodium cholate, 0.5 M KCl. The four beta-oxidation enzyme activities of the washes and the last extract were assayed with substrates of various carbon chain lengths. Our data suggest that the last extract contains a novel acyl-CoA dehydrogenase and long-chain 3-hydroxyacyl-CoA dehydrogenase. A novel acyl-CoA dehydrogenase was purified. The molecular masses of the native enzyme and the subunit were estimated to be 150 and 71 kDa, respectively. One mole of enzyme contained 2 mole of FAD. These properties and immunochemical properties of the enzyme differed from those of three other acyl-CoA dehydrogenases: short-, medium-, and long-chain acyl-CoA dehydrogenases. Carbon chain length specificity of the enzyme differed from that of other acyl-CoA dehydrogenases. The enzyme was active toward CoA esters of long- and very-long-chain fatty acids, but not toward those of medium- and short-chain fatty acids. The specific enzyme activity was greater than 10 times that of long-chain acyl-CoA dehydrogenase when palmitoyl-CoA was used as substrate. We propose the name "very-long-chain acyl-CoA dehydrogenase" for this enzyme.
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PMID:Novel fatty acid beta-oxidation enzymes in rat liver mitochondria. I. Purification and properties of very-long-chain acyl-coenzyme A dehydrogenase. 173 Jun 32