Catalysis in Enzymatic Decarboxylations: Comparison of Selected Cofactor-dependent and Cofactor-independent Examples.
Catalysis in Enzymatic Decarboxylations: Comparison of Selected Cofactor-dependent and Cofactor-independent Examples.
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DOI：
10.1021/cs400272x
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发表时间：
2013-07-05
期刊：
影响因子：
12.9
通讯作者：
Patel, Hetalben
中科院分区：
文献类型：
--
作者：
Jordan, Frank;Patel, Hetalben
关键词：
本文综述了三种类型的酶脱羧非常不同的底物：（1）硫胺素二磷酸（ThDP）依赖性酶与2-含氧酸反应;（2）吡哆醛磷酸（PLP）依赖性酶与α-氨基酸反应;（3）没有已知的辅因子，乳清酸苷5 '-单磷酸脱羧酶（OMPDC）。虽然前两个类已经研究了很多年，在过去的十年中，这两个类的研究揭示了新颖的机械洞察力挑战公认的理解。酶OMPDC已经对试图解释在没有辅因子甚至金属离子的情况下1017倍速率加速的酶学家提出了挑战。对三种脱羧酶的现有证据进行比较，突出了一些共同特征和更多差异。脱羧酶领域仍然是一个有趣的和具有挑战性的一个机制酶学尽管大量的信息已经可用。
This review is focused on three types of enzymes decarboxylating very different substrates: (1) Thiamin diphosphate (ThDP)-dependent enzymes reacting with 2-oxo acids; (2) Pyridoxal phosphate (PLP)-dependent enzymes reacting with α-amino acids; and (3) An enzyme with no known co-factors, orotidine 5'-monophosphate decarboxylase (OMPDC). While the first two classes have been much studied for many years, during the past decade studies of both classes have revealed novel mechanistic insight challenging accepted understanding. The enzyme OMPDC has posed a challenge to the enzymologist attempting to explain a 1017-fold rate acceleration in the absence of cofactors or even metal ions. A comparison of the available evidence on the three types of decarboxylases underlines some common features and more differences. The field of decarboxylases remains an interesting and challenging one for the mechanistic enzymologist notwithstanding the large amount of information already available.
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影响因子：
2.9
作者：
Arjunan, P;Nemeria, N;Furey, W
通讯作者：
Furey, W
DOI：
10.1038/nsb1101-963
发表时间：
2001-11-01
期刊：
NATURE STRUCTURAL BIOLOGY
影响因子：
--
作者：
Burkhard, P;Dominici, P;Malashkevich, VN
通讯作者：
Malashkevich, VN
影响因子：
15
作者：
BEAK, P;SIEGEL, B
通讯作者：
SIEGEL, B
影响因子：
15
作者：
ALVAREZ, FJ;ERMER, J;SCHOWEN, RL
通讯作者：
SCHOWEN, RL
影响因子：
15
作者：
CAIN, AH;SULLIVAN, GR;ROBERTS, JD
通讯作者：
ROBERTS, JD