Glucosamine 6-phosphate synthase
From Proteopedia
(Difference between revisions)
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== Function == | == Function == | ||
| - | '''Glucosamine 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)<ref>PMID:8528769</ref>. G6PS | + | '''Glucosamine 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)<ref>PMID:8528769</ref>. 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]]. |
== Relevance == | == Relevance == | ||
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== Structural highlights == | == Structural highlights == | ||
| - | The sugar binding by G6PS induces conformational change of the enzyme. The sugar binding pocket is found in the interface between the synthase and the glutaminase domains of G6PS<ref>PMID:18295797</ref>. | + | The sugar binding by G6PS induces conformational change of the enzyme domains. The sugar binding pocket is found in the interface between the synthase and the glutaminase domains of G6PS<ref>PMID:18295797</ref>. |
==3D structures of glucosamine 6-phosphate synthase== | ==3D structures of glucosamine 6-phosphate synthase== | ||
Revision as of 11:16, 7 March 2016
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