恶臭假单胞菌利用烷烃菌株中质粒决定的乙醇脱氢酶活性
Plasmid-determined alcohol dehydrogenase activity in alkane-utilizing strains of Pseudomonas putida.
作者信息
Benson S, Shapiro J
出版信息
J Bacteriol. 1976 May;126(2):794-8. doi: 10.1128/jb.126.2.794-798.1976.
Abstract
We have identified an alcohol dehydrogenase activity in Pseudomonas putida strains carrying the CAM-OCT degradative plasmid that were grown on octane. The activity is nicotinamide adenine dinucleotide independent, sediments at 48,000 x g, and shows 20-fold greater activity with octanol rather than butanol as substrate. The enzyme is inducible by unoxidized alkane and is present only in strains that have the OCT plasmid genes for alkane degradation with a wild-type alcO locus. No analogous chromosomal dehydrogenase could be detected. Wild-type and actanol-negative mutants (alcA-) without plasmids both contain a constitutive nicotinamide adenine dinucleotide-linked soluble alcohol dehydrogenase activity. This means that alcA- mutants are cryptic for octanol oxidation and suggests that the particulate plasmid-coded alcohol dehydrogenase activity is active on surface- or membrane-bound substrate.
摘要
我们在携带CAM - OCT降解质粒且以辛烷为生长底物的恶臭假单胞菌菌株中鉴定出了一种乙醇脱氢酶活性。该活性不依赖烟酰胺腺嘌呤二核苷酸，在48,000 x g下可沉淀，以辛醇而非丁醇作为底物时活性高20倍。该酶可被未氧化的烷烃诱导，且仅存在于具有用于烷烃降解的OCT质粒基因及野生型alcO位点的菌株中。未检测到类似的染色体脱氢酶。无质粒的野生型和辛醇阴性突变体（alcA-）均含有组成型烟酰胺腺嘌呤二核苷酸连接的可溶性乙醇脱氢酶活性。这意味着alcA-突变体对辛醇氧化是隐性的，表明颗粒状质粒编码的乙醇脱氢酶活性作用于表面或膜结合的底物。
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