GMP synthase

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<StructureSection load='2vxo' size='400' side='right' caption='Structure of human GMP synthase dimer complex with xantosine 5-phosphate (stick model) and sulfate (PDB entry [[2vxo]])' scene=''>
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<StructureSection load='2vxo' size='400' side='right' caption='Structure of human GMP synthase dimer complex with xantosine 5-phosphate and sulfate (PDB entry [[2vxo]])' scene='51/516475/Cv/1'>
== Function ==
== Function ==
'''GMP synthase''' (GMPS) catalyzes the conversion of xantosine 5’-phosphate (XMP), ATP, glutamine and water to glutamate, GMP, AMP and diphosphate. GMPS is active in purine and glutamate metabolism<ref>PMID:24462112</ref>. GMPS is a bifunctional two-domain enzyme with the N-terminal glutaminase dominates extracts ammonia from glutamine and the C-terminal synthetase adds amine group to XMP to produce GMP.
'''GMP synthase''' (GMPS) catalyzes the conversion of xantosine 5’-phosphate (XMP), ATP, glutamine and water to glutamate, GMP, AMP and diphosphate. GMPS is active in purine and glutamate metabolism<ref>PMID:24462112</ref>. GMPS is a bifunctional two-domain enzyme with the N-terminal glutaminase dominates extracts ammonia from glutamine and the C-terminal synthetase adds amine group to XMP to produce GMP.

Revision as of 07:55, 21 March 2016

Structure of human GMP synthase dimer complex with xantosine 5-phosphate and sulfate (PDB entry 2vxo)

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Proteopedia Page Contributors and Editors (what is this?)

Michal Harel, Alexander Berchansky

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