化能自养型黄杆菌的果糖二磷酸酶同工酶
Fructosebisphosphatase isoenzymes of the chemoautotroph Xanthobacter flavus.
作者信息
van den Bergh E R, van der Kooij T A, Dijkhuizen L, Meijer W G
机构信息
Department of Microbiology, Groningen Biomolecular Sciences and Biotechnology Institute (GBB), University of Groningen, Haren, The Netherlands.
出版信息
J Bacteriol. 1995 Oct;177(20):5860-4. doi: 10.1128/jb.177.20.5860-5864.1995.
Abstract
Xanthobacter flavus employs two fructosebisphosphatase (FBPase)-sedoheptulosebisphosphatase (SBPase) enzymes. One of these is constitutively expressed and has a high FBPase-to-SBPase ratio. The alternative enzyme, which is encoded by cbbF, is induced during autotrophic growth. The cbbF gene was expressed in Escherichia coli, and the FBPase was purified to homogeneity. The purified enzyme has a specific FBPase activity of 114 mumol/min/mg of protein, a Michaelis constant for fructosebisphosphate of 3 microM, and a low FBPase-to-SBPase ratio. CbbF was activated by ATP and inhibited by Ca2+.
摘要
黄色黄杆菌利用两种果糖双磷酸酶（FBPase）-景天庚酮糖双磷酸酶（SBPase）。其中一种是组成型表达的，FBPase与SBPase的比例较高。由cbbF编码的另一种酶在自养生长过程中被诱导。cbbF基因在大肠杆菌中表达，其FBPase被纯化至同质。纯化后的酶具有114 μmol/分钟/毫克蛋白质的特异性FBPase活性，果糖双磷酸的米氏常数为3 μM，且FBPase与SBPase的比例较低。CbbF被ATP激活并被Ca2+抑制。
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