BIOSYNTHESIS OF URIDINE DIPHOSPHATE D-XYLOSE .3. URIDINE DIPHOSPHATE D-GLUCOSE DEHYDROGENASE OF CRYPTOCOCCUS LAURENTII
BIOSYNTHESIS OF URIDINE DIPHOSPHATE D-XYLOSE .3. URIDINE DIPHOSPHATE D-GLUCOSE DEHYDROGENASE OF CRYPTOCOCCUS LAURENTII
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DOI:
10.1021/bi00870a012
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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;ANKEL, E;FEINGOLD, DS
Uridine diphosphate D-glucose dehydrogenase (EC 1. 1. 1. 22) from Cryptococcus laurentii has been partially purified and its properties have been investigated. Uridine diphosphate D-glucose is a substrate; the diphosphoglucose derivatives of adenosine, cytidine, guanosine, and thymidine are not substrates. Nicotinamide-adenine dinucleotide (NAD), 3-acetylpyridine-AD, or thionicotinamide-AD are active as hydrogen acceptors; [alpha]-NAD, deamino-NAD, 3-formylpyridine-AD, 3-propionylpyridine-AD, and ethylnicotinate-AD are inactive. The pH optimum is in the range 7. 3-7. 8; Km is 0. 6 m[image] for both uridine diphosphate D-glucose and NAD. The enzyme is strongly and specifically inhibited by uridine diphosphate D-xylose; the inhibition can be reversed by increased concentrations of either uridine diphosphate D-glucose or NAD. These observations as well as kinetic studies show that the inhibition is allosteric.