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The ferredoxin-thioredoxin system of a green alga, Chlamydomonas reinhardtii: identification and characterization of thioredoxins and ferredoxin-thioredoxin reductase components.莱茵衣藻的铁氧化还原蛋白-硫氧还蛋白系统：硫氧还蛋白和铁氧化还原蛋白-硫氧还蛋白还原酶组分的鉴定与表征
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CbbR, a LysR-type transcriptional activator, is required for expression of the autotrophic CO2 fixation enzymes of Xanthobacter flavus.CbbR是一种LysR型转录激活因子，是黄杆菌自养二氧化碳固定酶表达所必需的。
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Complementation analysis and regulation of CO2 fixation gene expression in a ribulose 1,5-bisphosphate carboxylase-oxygenase deletion strain of Rhodospirillum rubrum.红螺菌核糖-1,5-二磷酸羧化酶-加氧酶缺失菌株中二氧化碳固定基因表达的互补分析与调控
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The Calvin cycle enzyme phosphoglycerate kinase of Xanthobacter flavus required for autotrophic CO2 fixation is not encoded by the cbb operon.黄杆菌自养固定二氧化碳所需的卡尔文循环酶磷酸甘油酸激酶不是由cbb操纵子编码的。
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Action of calcium ions on spinach (Spinacia oleracea) chloroplast fructose bisphosphatase and other enzymes of the Calvin cycle.钙离子对菠菜（Spinacia oleracea）叶绿体果糖二磷酸酶及卡尔文循环其他酶的作用。
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Purification and regulatory properties of fructose 1,6-diphosphatase from Hydrogenomonas eutropha.嗜氢营养菌中果糖1,6 - 二磷酸酶的纯化及调节特性
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Characterization of Xanthobacter strains H4-14 and 25a and enzyme profiles after growth under autotrophic and heterotrophic conditions.嗜黄杆菌菌株H4-14和25a的特性以及在自养和异养条件下生长后的酶谱。
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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.

DOI:10.1128/jb.177.20.5860-5864.1995
PMID:7592335
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC177410/
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。