Mechanistic diversity in the RuBisCO superfamily: RuBisCO from Rhodospirillum rubrum is not promiscuous for reactions catalyzed by RuBisCO-like proteins.

Mechanistic diversity in the RuBisCO superfamily: RuBisCO from Rhodospirillum rubrum is not promiscuous for reactions catalyzed by RuBisCO-like proteins.
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DOI:
10.1021/bi301311t
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发表时间:
2012-11-27
期刊:
影响因子:
2.9
通讯作者:
Gerlt JA
Gerlt JA
中科院分区:
生物学3区
文献类型:
--
作者:
Warlick BP;Imker HJ;Sriram J;Tabita FR;Gerlt JA

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D-核酮糖1,5-二磷酸羧化酶/加氧酶(RuBisCOs)是一种混杂的酶,不仅催化D-核酮糖1,5-二磷酸的羧化和加氧,而且催化由D-核酮糖1,5-二磷酸的3-质子提取引发的其他混杂的、推测为非生理性的反应。此外,RuBisCO具有不催化羧化的同系物;这些被称为RuBisCO样蛋白或RLP。两个家族的RLP催化多胺合成产生的5′-甲硫基腺苷(MTA)的再循环反应:1)2,3-二酮基-5-甲硫基戊烷1-磷酸(DK-MTP 1-P)芽孢杆菌属物种中众所周知的“甲硫氨酸补救”途径中的“烯醇化酶”反应;和2)最近发现的“MTA-类异戊二烯分流”中的5-甲硫基-D-核酮糖1-磷酸(MTRU 1-P)1,3-异构酶反应,产生1-脱氧-D-木酮糖5-磷酸(DXP),用于红色红螺菌中非甲羟戊酸异戊二烯合成。我们首先研究了DK-MTP 1-P的结构和反应性,据报道其快速分解[Ashida,H.,Saito,Y.,Kojima,C.,和Yokota,A.等(2008)Biosci Biotechnol Biochem 72,959-67]。DK-MTP 1-P的2-羰基在溶液中快速水合,并且可以通过存在的少量未水合物质进行非酶促和酶促烯醇化。然后,我们检查了RuBisCO从R.红色催化RLP催化的两个反应。与以前的报告相反[Ashida,H.,齐藤,Y.,Kojima,C.,小林,K.,小笠原,N.,和Yokota,A.(2003)Science 302,286-290],我们不能证实该RuBisCO在体外或体内催化DK-MTP 1-P“烯醇化酶”反应。我们还确定该RuBisCO在体外不催化MTRU 1-P 1,3-异构酶反应。因此,尽管RuBisCO可以是功能上混杂的,但来自R.红色对于任何已知的RLP催化的反应都不是混杂的。
D-Ribulose 1,5-bisphosphate carboxylase/oxygenases (RuBisCOs) are promiscuous, catalyzing not only carboxylation and oxygenation of D-ribulose 1,5-bisphosphate but also other promiscuous, presumably nonphysiological, reactions initiated by abstraction of the 3-proton of D-ribulose 1,5-bisphosphate. Also, RuBisCO has homologues that do not catalyze carboxylation; these are designated RuBisCO-like proteins or RLPs. Members of the two families of RLPs catalyze reactions in the recycling of 5′-methylthioadenosine (MTA) generated by polyamine synthesis: 1) the 2,3-diketo-5-methylthiopentane 1-phosphate (DK-MTP 1-P) “enolase” reaction in the well-known “methionine salvage” pathway in species of Bacilli; and 2) the 5-methylthio-D-ribulose 1-phosphate (MTRu 1-P) 1,3-isomerase reaction in the recently discovered “MTA-isoprenoid shunt” that generates 1-deoxy-D-xylulose 5-phosphate (DXP) for nonmevalonate isoprene synthesis in Rhodospirillum rubrum. We first studied the structure and reactivity of DK-MTP 1-P which was reported to decompose rapidly [Ashida, H., Saito, Y., Kojima, C., and Yokota, A. (2008) Biosci Biotechnol Biochem 72, 959–67]. The 2-carbonyl group of DK-MTP 1-P is rapidly hydrated in solution and can undergo enolization both nonenzymatically and enzymatically via the small amount of unhydrated material that is present. We then examined the ability of RuBisCO from R. rubrum to catalyze both of the RLP-catalyzed reactions. Contrary to a previous report [Ashida, H., Saito, Y., Kojima, C., Kobayashi, K., Ogasawara, N., and Yokota, A. (2003) Science 302, 286–290], we were unable to confirm that this RuBisCO catalyzes the DK-MTP 1-P “enolase” reaction either in vitro or in vivo. We also determined that this RuBisCO does not catalyze the MTRu 1-P 1,3-isomerase reaction in vitro. Thus, although RuBisCOs can be functionally promiscuous, RuBisCO from R. rubrum is not promiscuous for either of the known RLP-catalyzed reactions.
DOI: 10.1021/bi7000483
发表时间: 2007-04-03
期刊: BIOCHEMISTRY
影响因子: 2.9
作者:
Imker, Heidi J.;Fedorov, Alexander A.;Gerlt, John A.
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