Enzymes regulated via cystathionine β-synthase domains
- 作者: Anashkin V.1, Baykov A.1, Lahti R.2
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隶属关系:
- Belozersky Institute of Physico-Chemical Biology
- Department of Biochemistry
- 期: 卷 82, 编号 10 (2017)
- 页面: 1079-1087
- 栏目: Review
- URL: https://journals.rcsi.science/0006-2979/article/view/151475
- DOI: https://doi.org/10.1134/S0006297917100017
- ID: 151475
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详细
Cystathionine β-synthase (CBS) domains discovered 20 years ago can bind different adenosine derivatives (AMP, ADP, ATP, S-adenosylmethionine, NAD, diadenosine polyphosphates) and thus regulate the activities of numerous proteins. Mutations in CBS domains of enzymes and membrane transporters are associated with several hereditary diseases. The regulatory unit is a quartet of CBS domains that belong to one or two polypeptides and usually form a conserved disk-like structure. CBS domains function as “internal inhibitors” in enzymes, and their bound ligands either amplify or attenuate the inhibitory effect. Recent studies have opened a way to understanding the structural basis of enzyme regulation via CBS domains and widened the list of their bound ligands.
作者简介
V. Anashkin
Belozersky Institute of Physico-Chemical Biology
Email: baykov@genebee.msu.ru
俄罗斯联邦, Moscow, 119992
A. Baykov
Belozersky Institute of Physico-Chemical Biology
编辑信件的主要联系方式.
Email: baykov@genebee.msu.ru
俄罗斯联邦, Moscow, 119992
R. Lahti
Department of Biochemistry
Email: baykov@genebee.msu.ru
芬兰, Turku, FIN-20014