Cloned (Comment) | Organism |
---|---|
gene Rv1389c | Mycobacterium tuberculosis |
KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
additional information | - |
additional information | detailed reaction kinetics, overview | Mycobacterium tuberculosis |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
ATP + GMP | Mycobacterium tuberculosis | guanylate kinase is an essential enzyme | ADP + GDP | - |
? | |
ATP + GMP | Mycobacterium tuberculosis H37Rv | guanylate kinase is an essential enzyme | ADP + GDP | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Mycobacterium tuberculosis | - |
- |
- |
Mycobacterium tuberculosis | P9WKE9 | Rv1389c gene | - |
Mycobacterium tuberculosis H37Rv | P9WKE9 | Rv1389c gene | - |
Posttranslational Modification | Comment | Organism |
---|---|---|
additional information | As is evident from the structure, GK has a clamp-like cavity, where the two lobes of the protein close through an ca. 1-nm conformational change upon binding the substrates, most of the conformational motion is induced by GMP binding. The substrates GMP and ATP drive this conformational change through several direct and indirect (via water molecules) interactions that bring the LID and nucleotide-monophosphate-binding domain (herein referred to as NMP-BD) nearer and jointly toward the CORE region, the structure closing in a vise-like motion. In this configuration, the CORE is catalytically active toward phosphoryl transfer, which relies on a residue sequence (the P-loop) that is conserved in kinases. | Mycobacterium tuberculosis |
Reaction | Comment | Organism | Reaction ID |
---|---|---|---|
ATP + GMP = ADP + GDP | conformational changes and induced-fit reaction mechanism of the allosteric enzyme, overview | Mycobacterium tuberculosis |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
ATP + GMP | guanylate kinase is an essential enzyme | Mycobacterium tuberculosis | ADP + GDP | - |
? | |
ATP + GMP | upon substrate binding, the LID and nucleotide-monophosphate-binding domains are brought together and toward the CORE with large concerted movements about the alpha3, helix 3, axis | Mycobacterium tuberculosis | ADP + GDP | - |
? | |
ATP + GMP | guanylate kinase is an essential enzyme | Mycobacterium tuberculosis H37Rv | ADP + GDP | - |
? | |
ATP + GMP | upon substrate binding, the LID and nucleotide-monophosphate-binding domains are brought together and toward the CORE with large concerted movements about the alpha3, helix 3, axis | Mycobacterium tuberculosis H37Rv | ADP + GDP | - |
? | |
guanosine monophosphate + adenosine triphosphate | Guanylate kinase (GK) is an essential enzyme that catalyzes the transfer of a phosphate from adenosine triphosphate (ATP) to guanosine monophosphate (GMP). | Mycobacterium tuberculosis | guanosine diphosphate + adenosine diphosphate | - |
? | |
additional information | the enzyme forms complexes with DNA | Mycobacterium tuberculosis | ? | - |
? | |
additional information | the enzyme forms complexes with DNA | Mycobacterium tuberculosis H37Rv | ? | - |
? |
Synonyms | Comment | Organism |
---|---|---|
guanylate kinase | - |
Mycobacterium tuberculosis |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
ATP | - |
Mycobacterium tuberculosis |