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甲醇氧化细菌中纯化的伯醇脱氢酶的底物特异性。

Substrate specificity of the purified primary alcohol dehydrogenases from methanol-oxidizing bacteria.

作者信息

Sperl G T, Forrest H S, Gibson D T

出版信息

J Bacteriol. 1974 May;118(2):541-50. doi: 10.1128/jb.118.2.541-550.1974.

DOI:10.1128/jb.118.2.541-550.1974
PMID:4828309
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC246787/
Abstract

Hyphomicrobium strain WC, Pseudomonas strain TP-1, and Pseudomonas strain W1 are capable of growth on methanol as the sole source of carbon and energy. Methanol-grown cells of each organism contain a primary alcohol dehydrogenase that has been purified to homogeneity. Each enzyme has a molecular weight of 120,000 and shows an in vitro requirement for phenazine methosulfate and ammonium ions for enzymatic activity. Normal aliphatic alcohols are oxidized rapidly by each enzyme. The presence of a methyl group on the carbon atom adjacent to the primary alcohol group lowers the enzymatic activity. This effect is reduced as the methyl substituent is moved further away from the hydroxyl group. The effect of other substituents on enzymatic activity is reported. Methanol, formaldehyde, and to a limited extent acetaldehyde are oxidized by the primary alcohol dehydrogenases. Higher aldehydes are not oxidized. A possible explanation for this specificity, with regard to aldehydes, is presented in terms of degree of hydration of the aldehyde.

摘要

分支微杆菌WC菌株、假单胞菌TP - 1菌株和假单胞菌W1菌株能够以甲醇作为唯一的碳源和能源生长。每种微生物在甲醇中生长的细胞都含有一种已纯化至同质的伯醇脱氢酶。每种酶的分子量为120,000,并且在体外表现出对硫酸吩嗪和铵离子的酶活性需求。正常脂肪醇可被每种酶快速氧化。与伯醇基团相邻的碳原子上存在甲基会降低酶活性。随着甲基取代基离羟基越远,这种效应会减弱。还报道了其他取代基对酶活性的影响。甲醇、甲醛以及在一定程度上乙醛可被伯醇脱氢酶氧化。高级醛则不被氧化。针对醛类的这种特异性,从醛的水合程度方面给出了一种可能的解释。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/ad3e/246787/80e5db331737/jbacter00341-0238-a.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/ad3e/246787/80e5db331737/jbacter00341-0238-a.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/ad3e/246787/80e5db331737/jbacter00341-0238-a.jpg

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