BIOSYNTHESIS OF URIDINE DIPHOSPHATE D-XYLOSE .2. URIDINE DIPHOSPHATE D-GLUCURONATE CARBOXY-LYASE OF CRYPTOCOCCUS LAURENTII
BIOSYNTHESIS OF URIDINE DIPHOSPHATE D-XYLOSE .2. URIDINE DIPHOSPHATE D-GLUCURONATE CARBOXY-LYASE OF CRYPTOCOCCUS LAURENTII
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DOI:
10.1021/bi00865a024
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发表时间:
1966-01-01
期刊:
影响因子:
2.9
通讯作者:
FEINGOLD, DS
中科院分区:
文献类型:
--
作者:
ANKEL, H;FEINGOLD, DS
Uridine diphosphate D-glucuronate carboxy-lyase of Cryptococcus laurentii has been partially purified and its properties have been investigated. Uridine diphosphate D-xylose and carbon dioxide are the only products of enzyme action. The pH optimum is between 7.0 and 7.5. Km for uridine diphosphate D-glucuronic acid is 1.1 x 10-3 [image]; the enzyme has an absolute and specific requirement for nicotinamide-adenine dinucleotide (NAD); Ka = 3 x 10-6 [image]. Reduced nicotinamide-adenine dinucleotide inhibits competitively with NAD; Ki = 2 x 10-6 [image]. The enzyme is inhibited by p-mercuribenzoate; the inhibition is reversed by cysteine. Label is retained when uridine diphosphate D-glucuronate-3-t or -4-t is decarboxylated by the enzyme.