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Literature summary for 2.7.4.8 extracted from

  • Zhang, Y.; Niu, H.; Li, Y.; Chu, H.; Shen, H.; Zhang, D.; Li, G.
    Mechanistic insight into the functional transition of the enzyme guanylate kinase induced by a single mutation (2015), Sci. Rep., 5, 8405.
    View publication on PubMedView publication on EuropePMC
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Protein Variants

Protein Variants Comment Organism
S35P the conversed proline residue at this position among all GK domains, drastically impairs the GMP binding affinity and significantly reduces the guanylate kinase activity, functional transition of the enzyme guanylate kinase is induced by a single mutation leading to the functional transition of the enzyme from a phosphoryl transfer kinase into a phosphorprotein interaction domain, molecular dynamic and metadynamics simulations, overview. The serine to proline mutation can also lead to the misrecognition of GMP, explaining the catalytic inactivity of the mutant. The GK domain is in an open state in the S35P mutant Saccharomyces cerevisiae

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+ required Saccharomyces cerevisiae

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
ATP + GMP Saccharomyces cerevisiae
-
 ADP + GDP
-
 ?

Organism

Organism UniProt Comment Textmining
Saccharomyces cerevisiae P15454
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + GMP
-
 Saccharomyces cerevisiae ADP + GDP
-
 ?
additional information functionally, the guanylate kinase domain is able to interact with a variety of phospho-peptide ligands with high affinity but its binding ability to GMP is low Saccharomyces cerevisiae ?
-
 ?

Cofactor

Cofactor Comment Organism Structure
ATP
-
 Saccharomyces cerevisiae

General Information

General Information Comment Organism
additional information the open-closed conformational transition in the wild-type enzyme is positive correlated with the process of GMP binding, indicating a GMP-induced closing motion of the enzyme. The GMP-bound enzyme maintains the fully closed state, in the presence of GMP, the inter-domain motions of GK enzyme are significantly restricted. Three residues Ser35, Glu70, and Asp101 more closely coordinate to the guanine ring of GMP. Structure modelling using structure PDB ID 1ex7 as a template Saccharomyces cerevisiae