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 | Comment | Organism | Structure |
---|---|---|---|
Mg2+ | required | Saccharomyces cerevisiae |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
ATP + GMP | Saccharomyces cerevisiae | - |
ADP + GDP | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Saccharomyces cerevisiae | P15454 | - |
- |
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 | Comment | Organism | Structure |
---|---|---|---|
ATP | - |
Saccharomyces cerevisiae |
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 |