AcsD catalyzes enantioselective citrate desymmetrization in siderophore biosynthesis.
AcsD catalyzes enantioselective citrate desymmetrization in siderophore biosynthesis.
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DOI:
10.1038/nchembio.145
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发表时间:
2009-03
影响因子:
14.8
通讯作者:
Naismith, James H.
中科院分区:
文献类型:
--
作者:
Schmelz, Stefan;Kadi, Nadia;McMahon, Stephen A.;Song, Lijiang;Oves-Costales, Daniel;Oke, Muse;Liu, Huanting;Johnson, Kenneth A.;Carter, Lester G.;Botting, Catherine H.;White, Malcolm F.;Challis, Gregory L.;Naismith, James H.
Bacterial pathogens need to scavenge iron from their host for growth and proliferation during infection. They have evolved several strategies to do this, one being the biosynthesis and excretion of small, high-affinity iron chelators known as siderophores. The biosynthesis of siderophores is an important area of study, not only for potential therapeutic intervention, but also to illuminate new enzyme chemistries. Two general pathways for siderophore biosynthesis exist: the well-characterized nonribosomal peptide synthetase (NRPS)-dependent pathway and the NRPS-independent (NIS) pathway, which relies on a different family of sparsely-investigated synthetases. Here, we report structural and biochemical studies of AcsD from Pectobacterium (formerly Erwinia) chrysanthemi, a NIS synthetase involved in achromobactin biosynthesis. The structures of ATP and citrate complexes provide a mechanistic rationale for stereospecific formation of an enzyme-bound (3R)-citryl-adenylate, which reacts with L-serine to form a likely achromobactin precursor. AcsD is a novel acyl adenylate-forming enzyme with a new fold and chemical catalysis strategy.
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影响因子:
4.8
作者:
Ginder, Nathaniel D.;Binkowski, Daniel J.;Honzatko, Richard B.
通讯作者:
Honzatko, Richard B.
DOI:
10.1107/s0907444904019158
发表时间:
2004-12-01
影响因子:
2.2
作者:
Emsley, P;Cowtan, K
通讯作者:
Cowtan, K
影响因子:
2.9
作者:
Jogl, G;Tong, L
通讯作者:
Tong, L
影响因子:
15
作者:
LIU, CF;TAM, JP
通讯作者:
TAM, JP
影响因子:
3.6
作者:
Cendrowski, S;MacArthur, W;Hanna, P
通讯作者:
Hanna, P