This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.
Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.
GMP synthase
From Proteopedia
(Difference between revisions)
| Line 1: | Line 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'> | <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 <scene name='51/516475/Cv/2'>N-terminal glutaminase</scene> dominates extracts ammonia from glutamine and the <scene name='51/516475/Cv/3'>C-terminal synthetase</scene> adds amine group to XMP to produce GMP. |
== Structural highlights == | == Structural highlights == | ||
Revision as of 08:01, 21 March 2016
| |||||||||||
