GMP synthase (glutamine-hydrolyzing) activity

Definition

Target type: molecularfunction

Catalysis of the reaction: ATP + XMP + L-glutamine + H2O = AMP + diphosphate + GMP + L-glutamate + 2H+. [RHEA:11680]

GMP synthase (glutamine-hydrolyzing) activity catalyzes the synthesis of guanosine monophosphate (GMP) from xanthosine monophosphate (XMP) and glutamine. This reaction is essential for the biosynthesis of purine nucleotides, which are building blocks for DNA and RNA. The enzyme utilizes glutamine as an ammonia donor and hydrolyzes it to glutamate, releasing ammonia. The ammonia then reacts with XMP, forming GMP. The reaction proceeds in two steps: 1) The enzyme binds to both XMP and glutamine, forming a ternary complex. 2) The enzyme then catalyzes the transfer of the ammonia group from glutamine to XMP, forming GMP and glutamate. The mechanism of the reaction involves the formation of a covalent intermediate between the enzyme and glutamine. This intermediate is then attacked by XMP, resulting in the formation of GMP and the release of glutamate. GMP synthase (glutamine-hydrolyzing) activity is a highly regulated enzyme, with its activity being controlled by the availability of substrates, feedback inhibition by GMP and other purine nucleotides, and allosteric regulation by various metabolites.'
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Proteins (2)

Compounds (2)