GMP synthase
From Proteopedia
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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'> | <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 <scene name='51/516475/Cv/ | + | '''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 <scene name='51/516475/Cv/12'>N-terminal glutaminase</scene> dominates extracts ammonia from glutamine and the <scene name='51/516475/Cv/13'>C-terminal synthetase</scene> adds amine group to XMP to produce GMP. |
== Structural highlights == | == Structural highlights == | ||
| - | Human GMPS structure contains <scene name='51/516475/Cv/ | + | Human GMPS structure contains <scene name='51/516475/Cv/14'>2 dimerization domains (D1 and D2)</scene>. The <scene name='51/516475/Cv/15'>active site is located between the synthetase domain and D2 domain and covered by the LID motif</scene>. <scene name='51/516475/Cv/16'>Whole active site</scene>. N-terminal glutaminase domain contains <scene name='51/516475/Cv/17'>catalytic triad Cys104, His190, Glu192</scene><ref>PMID:23816837</ref>. |
==3D structures of GMP synthase== | ==3D structures of GMP synthase== | ||
Revision as of 11:51, 3 April 2019
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