Intrigues and intricacies of the biosynthetic pathways for the enzymatic quinocofactors: PQQ, TTQ, CTQ, TPQ, and LTQ.
Intrigues and intricacies of the biosynthetic pathways for the enzymatic quinocofactors: PQQ, TTQ, CTQ, TPQ, and LTQ.
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DOI：
10.1021/cr400475g
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发表时间：
2014-04-23
期刊：
影响因子：
62.1
通讯作者：
Bonnot, Florence
中科院分区：
文献类型：
--
作者：
Klinman, Judith P.;Bonnot, Florence
蛋白质和核酸修饰过程在细胞活力中起核心作用。这些范围从通过DNA修饰调节转录，1翻译前RNA剪接，2和通过蛋白质共价修饰在多个水平上控制细胞信号传导，例如，参考文献3和4。还已知肽经历广泛的修饰，特别是在细菌产生细胞防御分子期间，越来越多地将其作为可能的哺乳动物抗生素进行研究。5这篇综述集中在一组独特的翻译后修饰，这些修饰将肽或折叠蛋白质内的典型氨基酸侧链转化为含醌的氧化还原辅因子。6，7肽衍生的醌辅因子吡咯喹啉醌（PQQ）是1964年首次发现的，与细菌酶葡萄糖脱氢酶有关。[8]随后对PQQ进行了X射线表征，无论是单独的还是与几种酶形成的非共价复合物。10− 12 PQQ是一种可逆结合的辅因子，可以在许多氧化还原蛋白质中共享，这一特性与图1中给出的其余醌辅因子形成对比，发现每一种醌辅因子都与其同源蛋白质共价结合。PQQ和其余醌辅因子的表征之间存在相当大的滞后，三羟基苯丙氨酸醌（TPQ）13和色氨酸醌（TTQ）14的鉴定发生在20世纪90年代初，随后是赖氨酰酪氨酸醌（LTQ）15在1996年和半胱氨酸醌（CTQ）16在2001年。发现这些醌辅因子在原核生物或真核生物中起作用，TPQ是跨越这两个生物学领域的例外。每个辅因子的区别特征在表1中突出显示，潜在的共同点是每个辅因子都围绕芳香族侧链（色氨酸或酪氨酸）构建。这篇综述主要关注quinocofactors生产的各种生物合成途径[cf.参考文献7、17和18]，并且读者可以参考主要集中在围绕成熟辅因子的酶机制上的许多论文。19− 21
Protein and nucleic acid modification processes play a central role in cellular viability. These range from the regulation of transcription via the modification of DNA, 1 the splicing of RNA prior to translation, 2 and the control of cell signaling at a multitude of levels via covalent modifications of proteins, eg, refs 3 and 4. Peptides are also known to undergo extensive modifications, in particular, during the bacterial generation of cellular defense molecules that are increasingly being studied as possible mammalian antibiotics. 5 This review is focused on a unique set of posttranslational modifications that convert canonical amino acid side chains within either a peptide or folded protein into quinonecontaining redox cofactors. 6, 7 The peptide-derived quinocofactor, pyrroloquinoline quinone (PQQ), was the first to be detected in 1964, in association with the bacterial enzyme, glucose dehydrogenase. 8 This was followed by X-ray characterizations of PQQ, either alone 9 or in a noncovalent complex with several dehydrogenases. 10− 12 The property of PQQ as a reversibly bound cofactor that can be shared among many redox proteins contrasts with the remaining quinocofactors presented in Scheme 1, each of which is found to be covalently associated with its cognate protein. There was a considerable lag between the characterization of PQQ and the remainder of the quinocofactors, with identification of trihydroxyphenylalanine quinone (TPQ) 13 and tryptophan tryptophylquinone (TTQ) 14 occurring in the early 1990s, followed by lysyl tyrosine quinone (LTQ) 15 in 1996 and cysteine tryptophylquinone (CTQ) 16 in 2001. These quinocofactors are found to function either in prokaryotes or eukaryotes, with TPQ being the exception that spans these two biological domains. The distinguishing features of each cofactor are highlighted in Table 1, with the underlying commonality being that each is constructed around an aromatic side chain (tryptophan or tyrosine). This review brings a primary focus to the variety of biosynthetic pathways for the production of quinocofactors [cf. refs 7, 17, and 18], and the reader is referred to a number of treatises that are centered primarily on the enzymatic mechanisms surrounding the mature cofactors. 19− 21
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DOI：
10.1016/s0006-291x(05)80007-5
发表时间：
1992-05-15
影响因子：
3.1
作者：
CHISTOSERDOV, AY;BOYD, J;LIDSTROM, ME
通讯作者：
LIDSTROM, ME
影响因子：
1.6
作者：
Adachi, O;Kubota, T;Matsushita, K
通讯作者：
Matsushita, K
影响因子：
13.8
作者：
Dandekar, T;Snel, B;Bork, P
通讯作者：
Bork, P
影响因子：
2.9
作者：
Chen, ZW;Schwartz, B;Mathews, FS
通讯作者：
Mathews, FS
DOI：
10.1038/nsb0294-102
发表时间：
1994-02-01
期刊：
NATURE STRUCTURAL BIOLOGY
影响因子：
--
作者：
BLAKE, CCF;GHOSH, M;ANTHONY, C
通讯作者：
ANTHONY, C