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Purification and properties of nicotinamide mononucleotide amidohydrolase from Azotobacter vinelandii.

作者信息

Imai T

出版信息

J Biochem. 1973 Jan;73(1):139-53.

PMID:4144084
Abstract
摘要

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1
Purification and properties of nicotinamide mononucleotide amidohydrolase from Azotobacter vinelandii.来自棕色固氮菌的烟酰胺单核苷酸酰胺水解酶的纯化及性质
J Biochem. 1973 Jan;73(1):139-53.
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Nicotinamide adenine dinucleotide kinase from Azotobacter vinelandii cells. A possible mechanism for the enzyme reaction.来自棕色固氮菌细胞的烟酰胺腺嘌呤二核苷酸激酶。酶反应的一种可能机制。
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[Purification and characterization of the polynucleotide phosphorylase of Azotobacter vinelandii].[棕色固氮菌多核苷酸磷酸化酶的纯化与特性分析]
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Characterization and mutational analysis of a nicotinamide mononucleotide deamidase from Agrobacterium tumefaciens showing high thermal stability and catalytic efficiency.来自根癌农杆菌的烟酰胺单核苷酸脱酰胺酶的表征及突变分析,该酶具有高热稳定性和催化效率。
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烟酰胺单核苷酸脱酰胺酶系统发育和分子分类的新见解。
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Identification of nicotinamide mononucleotide deamidase of the bacterial pyridine nucleotide cycle reveals a novel broadly conserved amidohydrolase family.鉴定细菌吡啶核苷酸循环中的烟酰胺单核苷酸脱氨酶揭示了一种新型广泛保守的酰胺水解酶家族。
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Microbiol Rev. 1980 Mar;44(1):83-105. doi: 10.1128/mr.44.1.83-105.1980.
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J Bacteriol. 1982 Dec;152(3):1111-6. doi: 10.1128/jb.152.3.1111-1116.1982.