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Literature summary extracted from

  • Choi, B.; Zocchi, G.
    Guanylate kinase, induced fit, and the allosteric spring probe (2007), Biophys. J., 92, 1651-1658.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
2.7.4.8 gene Rv1389c Mycobacterium tuberculosis

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
2.7.4.8 additional information
-
 additional information detailed reaction kinetics, overview Mycobacterium tuberculosis

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2.7.4.8 ATP + GMP Mycobacterium tuberculosis guanylate kinase is an essential enzyme ADP + GDP
-
 ?
2.7.4.8 ATP + GMP Mycobacterium tuberculosis H37Rv guanylate kinase is an essential enzyme ADP + GDP
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
2.7.4.8 Mycobacterium tuberculosis
-
-
-
2.7.4.8 Mycobacterium tuberculosis P9WKE9 Rv1389c gene
-
2.7.4.8 Mycobacterium tuberculosis H37Rv P9WKE9 Rv1389c gene
-

Posttranslational Modification

EC Number Posttranslational Modification Comment Organism
2.7.4.8 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

EC Number Reaction Comment Organism Reaction ID
2.7.4.8 ATP + GMP = ADP + GDP conformational changes and induced-fit reaction mechanism of the allosteric enzyme, overview Mycobacterium tuberculosis
a

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.7.4.8 ATP + GMP guanylate kinase is an essential enzyme Mycobacterium tuberculosis ADP + GDP
-
 ?
2.7.4.8 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
-
 ?
2.7.4.8 ATP + GMP guanylate kinase is an essential enzyme Mycobacterium tuberculosis H37Rv ADP + GDP
-
 ?
2.7.4.8 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
-
 ?
2.7.4.8 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
-
 ?
2.7.4.8 additional information the enzyme forms complexes with DNA Mycobacterium tuberculosis ?
-
 ?
2.7.4.8 additional information the enzyme forms complexes with DNA Mycobacterium tuberculosis H37Rv ?
-
 ?

Synonyms

EC Number Synonyms Comment Organism
2.7.4.8 guanylate kinase
-
 Mycobacterium tuberculosis

Cofactor

EC Number Cofactor Comment Organism Structure
2.7.4.8 ATP
-
 Mycobacterium tuberculosis