Glucosamine 6-phosphate synthase: Difference between revisions
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[[2vf4]] - EcG6PS – ''Escherichia coli''<br /> | [[2vf4]] - EcG6PS – ''Escherichia coli''<br /> | ||
[[3tbf]] – G6PS C terminal – ''Francisella tularensis''<br /> | [[3tbf]] – G6PS C terminal – ''Francisella tularensis''<br /> | ||
[[1moq]], [[2vf5]] – EcG6PS + G6P<br /> | [[1moq]], [[2vf5]], [[1mor]], [[1jxa]] – EcG6PS + G6P<br /> | ||
[[ | [[4amv]] – EcG6PS + F6P<br /> | ||
[[1xff]] - EcG6PS glutaminase domain + glutamate<br /> | [[1xff]] - EcG6PS glutaminase domain + glutamate<br /> | ||
[[1xfg]] - EcG6PS glutaminase domain + glutamic hydroxamate<br /> | [[1xfg]] - EcG6PS glutaminase domain + glutamic hydroxamate<br /> | ||
[[1mos]] – EcG6PS + ADGP<br /> | [[1mos]] – EcG6PS + ADGP<br /> | ||
[[ | [[2j6h]] - EcG6PS + oxo-norleucine + G6P<br /> | ||
[[ | [[2puv]] – CaG6PS isomerase domain + uridine-2P-acetylglucosamine – ''Candida albicans''<br /> | ||
[[2put]] – CaG6PS isomerase domain + uridine-2P-acetylglucosamine + F6P<br /> | |||
[[2puw]] – CaG6PS isomerase domain + glucopyranose<br /> | |||
[[2poc]] – CaG6PS isomerase domain + uridine-2P-acetylglucosamine + glucopyranose<br /> | |||
== References == | == References == | ||
<references/> | <references/> | ||
[[Category:Topic Page]] | [[Category:Topic Page]] | ||
Revision as of 11:44, 3 August 2020
FunctionGlucosamine 6-phosphate synthase (G6PS) catalyzes the first step in the biosynthesis of UDP-GlcNAc. G6PS converts fructose-6-phosphate (F6P) and glutamine to glucosamine-6-phosphate (G6P)[1]. G6PS consists of two domains which catalyze two reactions. The N-terminal glutaminase domain (E.coli residues 2-239) which catalyzes the hydrolysis of glutamine to glutamate and ammonia which is transferred to F6P and the C-terminal synthase domain (E.coli residues 248-end) which catalyzes the isomerization of F6P from ketose to aldose. The most potent inhibitor of G6PS is the intermediate analog amino-2-deoxy-D-glucitol 6-phosphate (ADGP). See also Isomerases. RelevanceN-acetylglucosamine is an essential building block of chitin which comprises the bacterial and fungal cell wall. Hence, G6PS is a target to anti-bacterial and anti-fungal agents. Structural highlightsThe sugar binding by G6PS induces conformational change of the enzyme domains. . The is found in the interface between the synthase and the glutaminase domains of G6PS[2]. |
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3D structures of glucosamine 6-phosphate synthase3D structures of glucosamine 6-phosphate synthase
Updated on 03-August-2020
2vf4 - EcG6PS – Escherichia coli
3tbf – G6PS C terminal – Francisella tularensis
1moq, 2vf5, 1mor, 1jxa – EcG6PS + G6P
4amv – EcG6PS + F6P
1xff - EcG6PS glutaminase domain + glutamate
1xfg - EcG6PS glutaminase domain + glutamic hydroxamate
1mos – EcG6PS + ADGP
2j6h - EcG6PS + oxo-norleucine + G6P
2puv – CaG6PS isomerase domain + uridine-2P-acetylglucosamine – Candida albicans
2put – CaG6PS isomerase domain + uridine-2P-acetylglucosamine + F6P
2puw – CaG6PS isomerase domain + glucopyranose
2poc – CaG6PS isomerase domain + uridine-2P-acetylglucosamine + glucopyranose
ReferencesReferences
- ↑ White SH, Wimley WC, Selsted ME. Structure, function, and membrane integration of defensins. Curr Opin Struct Biol. 1995 Aug;5(4):521-7. PMID:8528769
- ↑ Mouilleron S, Badet-Denisot MA, Golinelli-Pimpaneau B. Ordering of C-terminal loop and glutaminase domains of glucosamine-6-phosphate synthase promotes sugar ring opening and formation of the ammonia channel. J Mol Biol. 2008 Apr 4;377(4):1174-85. Epub 2008 Feb 4. PMID:18295797 doi:10.1016/j.jmb.2008.01.077