Mechanistic diversity in the RuBisCO superfamily: a novel isomerization reaction catalyzed by the RuBisCO-like protein from Rhodospirillum rubrum.

Mechanistic diversity in the RuBisCO superfamily: a novel isomerization reaction catalyzed by the RuBisCO-like protein from Rhodospirillum rubrum.
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DOI:
10.1021/bi801685f
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发表时间:
2008-10-28
期刊:
影响因子:
2.9
通讯作者:
Gerlt, John A.
Gerlt, John A.
中科院分区:
生物学3区
文献类型:
--
作者:
Imker, Heidi J.;Singh, Jaya;Warlick, Benjamin P.;Tabita, F. Robert;Gerlt, John A.

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D-核酮糖1,5-二磷酸羧化酶/加氧酶(Rubisco)的某些同系物不催化羧化,被命名为Rubisco样蛋白(RLPs)。红色红螺菌RLP(gI:83593333)催化一种新的异构化反应(总的1,3-质子转移反应,可能是两个1,2-质子转移反应),将5-甲硫基-D-核酮糖1-磷酸转化为1-甲硫基-5-磷酸和1-甲硫代核酮糖5-磷酸的3:1混合物。RLP编码基因的中断使红色红假单胞菌不能利用5‘-甲硫腺苷作为唯一的硫源,这意味着一条新的、尚未确定的硫回收途径。
Some homologues of D-ribulose 1,5-bisphosphate carboxylase/oxygenase (RuBisCO) do not catalyze carboxylation and are designated RuBisCO-like proteins (RLPs). The RLP from Rhodospirillum rubrum (gi:83593333) catalyzes a novel isomerization reaction (overall 1,3-proton transfer reaction; likely, two 1,2-proton transfer reactions) that converts 5-methylthio-D-ribulose 1-phosphate to a 3:1 mixture of 1-methylthio-xylulose 5-phosphate and 1-methylthioribulose 5-phosphate. Disruption of the gene encoding the RLP abolishes the ability of R. rubrum to utilize 5′-methylthioadenosine as sole sulfur source, implicating a new, as yet uncharacterized, pathway for sulfur salvage.
DOI: 10.1021/bi7000483
发表时间: 2007-04-03
期刊: BIOCHEMISTRY
影响因子: 2.9
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