TrpB2 Enzymes are O-Phospho-L-serine Dependent Tryptophan Synthases

被引：9

作者：

Busch, Florian ^{[1
]}

Rajendran, Chitra ^{[1
]}

Mayans, Olga ^{[2
]}

Loeffler, Patrick ^{[1
]}

Merkl, Rainer ^{[1
]}

Sterner, Reinhard ^{[1
]}

机构：

[1] Univ Regensburg, Inst Biophys & Phys Biochem, D-93053 Regensburg, Germany

[2] Univ Liverpool, Inst Integrat Biol, Liverpool L69 7ZB, Merseyside, England

来源：

BIOCHEMISTRY | 2014年 / 53卷 / 38期

关键词：

HYPERTHERMOPHILIC ARCHAEON; BETA-SUBUNIT; ACETYLSERINE SULFHYDRYLASE; 3-DIMENSIONAL STRUCTURE; BIENZYME COMPLEX; ACTIVE-SITES; INDOLE; BIOSYNTHESIS; COMMUNICATION; MUTATIONS;

D O I：

10.1021/bi500977y

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

070307 [化学生物学]; 071010 [生物化学与分子生物学];

摘要：

The rapid increase of the number of sequenced genomes asks for the functional annotation of the encoded enzymes. We used a combined computational-structural approach to determine the function of the TrpB2 subgroup of the tryptophan synthase beta chain/beta chain-like TrpB1-TrpB2 family (IPR023026). The results showed that TrpB2 enzymes are O-phospho-l-serine dependent tryptophan synthases, whereas TrpB1 enzymes catalyze the l-serine dependent synthesis of tryptophan. We found a single residue being responsible for the different substrate specificities of TrpB1 and TrpB2 and confirmed this finding by mutagenesis studies and crystallographic analysis of a TrpB2 enzyme with bound O-phospho-l-serine.

引用

页码：6078 / 6083

页数：6

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