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Literature summary for 2.7.4.8 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
Search for more literature for 2.7.4.8

Cloned(Commentary)

Cloned (Comment) Organism
gene Rv1389c Mycobacterium tuberculosis

KM Value [mM]

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

Natural Substrates/ Products (Substrates)

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

Organism UniProt Comment Textmining
Mycobacterium tuberculosis
-
-
-
Mycobacterium tuberculosis P9WKE9 Rv1389c gene
-
Mycobacterium tuberculosis H37Rv P9WKE9 Rv1389c gene
-

Posttranslational Modification

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

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

Substrates and Products (Substrate)

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

Synonyms Comment Organism
guanylate kinase
-
 Mycobacterium tuberculosis

Cofactor

Cofactor Comment Organism Structure
ATP
-
 Mycobacterium tuberculosis