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β-碳酸酐酶的结构与催化机制

Structure and catalytic mechanism of the beta-carbonic anhydrases.

作者信息

Rowlett Roger S

机构信息

Colgate University, Department of Chemistry, Hamilton, NY 13346, USA.

出版信息

Biochim Biophys Acta. 2010 Feb;1804(2):362-73. doi: 10.1016/j.bbapap.2009.08.002. Epub 2009 Aug 11.

Abstract

The beta-carbonic anhydrases (beta-CAs) are a diverse but structurally related group of zinc-metalloenzymes found in eubacteria, plant chloroplasts, red and green algae, and in the Archaea. The enzyme catalyzes the rapid interconversion of CO(2) and H(2)O to HCO(3)(-) and H(+), and is believed to be associated with metabolic enzymes that consume or produce CO(2) or HCO(3)(-). For many organisms, beta-CA is essential for growth at atmospheric concentrations of CO(2). Of the five evolutionarily distinct classes of carbonic anhydrase, beta-CA is the only one known to exhibit allosterism. Here we review the structure and catalytic mechanism of beta-CA, including the structural basis for allosteric regulation.

摘要

β-碳酸酐酶(β-CAs)是一组多样但结构相关的锌金属酶,存在于真细菌、植物叶绿体、红藻和绿藻以及古生菌中。该酶催化CO₂和H₂O快速相互转化为HCO₃⁻和H⁺,并被认为与消耗或产生CO₂或HCO₃⁻的代谢酶有关。对于许多生物体而言,β-碳酸酐酶对于在大气CO₂浓度下生长至关重要。在碳酸酐酶的五个进化上不同的类别中,β-碳酸酐酶是已知唯一表现出别构效应的一类。在此,我们综述β-碳酸酐酶的结构和催化机制,包括别构调节的结构基础。

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