1i7q
From Proteopedia
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{{STRUCTURE_1i7q| PDB=1i7q | SCENE= }} | {{STRUCTURE_1i7q| PDB=1i7q | SCENE= }} | ||
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===ANTHRANILATE SYNTHASE FROM S. MARCESCENS=== | ===ANTHRANILATE SYNTHASE FROM S. MARCESCENS=== | ||
| + | {{ABSTRACT_PUBMED_11371633}} | ||
| - | + | ==Function== | |
| - | + | [[http://www.uniprot.org/uniprot/TRPE_SERMA TRPE_SERMA]] Part of a heterotetrameric complex that catalyzes the two-step biosynthesis of anthranilate, an intermediate in the biosynthesis of L-tryptophan. In the first step, the glutamine-binding beta subunit (TrpG) of anthranilate synthase (AS) provides the glutamine amidotransferase activity which generates ammonia as a substrate that, along with chorismate, is used in the second step, catalyzed by the large alpha subunit of AS (TrpE) to produce anthranilate. In the absence of TrpG, TrpE can synthesize anthranilate directly from chorismate and high concentrations of ammonia (Probable). [[http://www.uniprot.org/uniprot/TRPG_SERMA TRPG_SERMA]] Part of a heterotetrameric complex that catalyzes the two-step biosynthesis of anthranilate, an intermediate in the biosynthesis of L-tryptophan. In the first step, the glutamine-binding beta subunit (TrpG) of anthranilate synthase (AS) provides the glutamine amidotransferase activity which generates ammonia as a substrate that, along with chorismate, is used in the second step, catalyzed by the large alpha subunit of AS (TrpE) to produce anthranilate. In the absence of TrpG, TrpE can synthesize anthranilate directly from chorismate and high concentrations of ammonia (Probable).<ref>PMID:11371633</ref> | |
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==About this Structure== | ==About this Structure== | ||
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==Reference== | ==Reference== | ||
| - | <ref group="xtra">PMID:011371633</ref><references group="xtra"/> | + | <ref group="xtra">PMID:011371633</ref><references group="xtra"/><references/> |
[[Category: Anthranilate synthase]] | [[Category: Anthranilate synthase]] | ||
[[Category: Serratia marcescens]] | [[Category: Serratia marcescens]] | ||
Revision as of 10:43, 16 April 2014
Contents |
ANTHRANILATE SYNTHASE FROM S. MARCESCENS
Template:ABSTRACT PUBMED 11371633
Function
[TRPE_SERMA] Part of a heterotetrameric complex that catalyzes the two-step biosynthesis of anthranilate, an intermediate in the biosynthesis of L-tryptophan. In the first step, the glutamine-binding beta subunit (TrpG) of anthranilate synthase (AS) provides the glutamine amidotransferase activity which generates ammonia as a substrate that, along with chorismate, is used in the second step, catalyzed by the large alpha subunit of AS (TrpE) to produce anthranilate. In the absence of TrpG, TrpE can synthesize anthranilate directly from chorismate and high concentrations of ammonia (Probable). [TRPG_SERMA] Part of a heterotetrameric complex that catalyzes the two-step biosynthesis of anthranilate, an intermediate in the biosynthesis of L-tryptophan. In the first step, the glutamine-binding beta subunit (TrpG) of anthranilate synthase (AS) provides the glutamine amidotransferase activity which generates ammonia as a substrate that, along with chorismate, is used in the second step, catalyzed by the large alpha subunit of AS (TrpE) to produce anthranilate. In the absence of TrpG, TrpE can synthesize anthranilate directly from chorismate and high concentrations of ammonia (Probable).[1]
About this Structure
1i7q is a 4 chain structure with sequence from Serratia marcescens. Full crystallographic information is available from OCA.
Reference
- Spraggon G, Kim C, Nguyen-Huu X, Yee MC, Yanofsky C, Mills SE. The structures of anthranilate synthase of Serratia marcescens crystallized in the presence of (i) its substrates, chorismate and glutamine, and a product, glutamate, and (ii) its end-product inhibitor, L-tryptophan. Proc Natl Acad Sci U S A. 2001 May 22;98(11):6021-6. PMID:11371633 doi:10.1073/pnas.111150298
- ↑ Spraggon G, Kim C, Nguyen-Huu X, Yee MC, Yanofsky C, Mills SE. The structures of anthranilate synthase of Serratia marcescens crystallized in the presence of (i) its substrates, chorismate and glutamine, and a product, glutamate, and (ii) its end-product inhibitor, L-tryptophan. Proc Natl Acad Sci U S A. 2001 May 22;98(11):6021-6. PMID:11371633 doi:10.1073/pnas.111150298
