Klingenberg M, Echtay K S
Institut für Physiologische Chemie der Universität München, Schillerstrasse 44, D-80336 Munich, Germany.
Biochim Biophys Acta. 2001 Mar 1;1504(1):128-43. doi: 10.1016/s0005-2728(00)00242-5.
The functional characteristics of uncoupling proteins (UCP) are reviewed, with the main focus on the results with isolated and reconstituted proteins. UCP1 from brown adipose tissue, the paradigm of the UCP subfamily, is treated in more detail. The issues addressed are the role and mechanism of fatty acids, the nucleotide binding, the regulation by pH and the identification by mutagenesis of residues involved in these functions. The transport and regulatory functions of UCP2 and 3 are reviewed in comparison to UCP1. The inconsistencies of a proposed nucleotide insensitive H(+) transport by these UCPs as concluded from the expression in yeast and Escherichia coli are elucidated. In both expression system UCP 2 and 3 are not in or cannot be converted to a functionally native state and thus also for these UCPs a nucleotide regulated H (+) transport is postulated.
本文综述了解偶联蛋白（UCP）的功能特性，主要关注分离和重组蛋白的研究结果。对棕色脂肪组织中的UCP1（UCP亚家族的典型代表）进行了更详细的探讨。涉及的问题包括脂肪酸的作用和机制、核苷酸结合、pH调节以及通过诱变鉴定参与这些功能的残基。将UCP2和UCP3的转运和调节功能与UCP1进行了比较。阐明了根据在酵母和大肠杆菌中的表达得出的关于这些UCP存在对核苷酸不敏感的H(+)转运这一观点的不一致之处。在这两种表达系统中，UCP2和UCP3都不处于或无法转化为功能上的天然状态，因此也推测这些UCP存在核苷酸调节的H(+)转运。
