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Literature summary extracted from

  • Arvind, A.; Jain, V.; Saravanan, P.; Mohan, C.G.
    Uridine monophosphate kinase as potential target for tuberculosis: from target to lead identification (2013), Interdiscip. Sci. Comput. Life Sci., 5, 296-311.
    View publication on PubMed

Activating Compound

EC Number Activating Compound Comment Organism Structure
2.7.4.22 GTP allosteric activation Mycobacterium tuberculosis

Application

EC Number Application Comment Organism
2.7.4.22 drug development the enzyme is a potential drug target for developing novel anti-tuberculosis drugs Mycobacterium tuberculosis

Cloned(Commentary)

EC Number Cloned (Comment) Organism
2.7.4.22 gene pyrH or Rv2883c, sequence comparisons and phylogenetic analysis and tree Mycobacterium tuberculosis

Inhibitors

EC Number Inhibitors Comment Organism Structure
2.7.4.22 1-[([5-oxo-4-[(2R)-tetrahydrofuran-2-ylmethyl]-4,5-dihydro-1H-1,2,4-triazol-3-yl]sulfanyl)acetyl]piperidine-4-carboxylic acid
-
 Mycobacterium tuberculosis
2.7.4.22 2-(4-acetyl-3,5-dimethyl-1H-pyrazol-1-yl)-N-[1-(2-methoxybenzyl)-1H-pyrazol-5-yl]acetamide
-
 Mycobacterium tuberculosis
2.7.4.22 4-[2-amino-4-(4-chlorophenyl)-7-oxo-5,7-dihydro-6H-pyrrolo[3,4-d]pyrimidin-6-yl]butanoic acid
-
 Mycobacterium tuberculosis
2.7.4.22 4-[2-amino-4-(4-methoxyphenyl)-7-oxo-5,7-dihydro-6H-pyrrolo[3,4-d]pyrimidin-6-yl]butanoic acid
-
 Mycobacterium tuberculosis
2.7.4.22 5-[(9H-[1,2,4]triazolo[4,3-a]benzimidazol-3-ylsulfanyl)methyl]furan-2-carboxylic acid hydrogen bonding interactions of ZINC12561276 molecule with the active site residues of Mtb-UMPK homology model, overview Mycobacterium tuberculosis
2.7.4.22 additional information structure-based inhibitor design, inhibitor screening and molecular docking study Mycobacterium tuberculosis
2.7.4.22 N-benzyl-2-[(2S,3R,4S,5R)-3,4-dihydroxy-5-[[(methylsulfonyl)amino]methyl]tetrahydrofuran-2-yl]-N-methylacetamide
-
 Mycobacterium tuberculosis
2.7.4.22 UTP physiological inhibitor Mycobacterium tuberculosis

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
2.7.4.22 Mg2+ required Mycobacterium tuberculosis

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2.7.4.22 ATP + UMP Mycobacterium tuberculosis
-
 ADP + UDP
-
 r
2.7.4.22 ATP + UMP Mycobacterium tuberculosis H37Rv
-
 ADP + UDP
-
 r

Organism

EC Number Organism UniProt Comment Textmining
2.7.4.22 Mycobacterium tuberculosis P9WHK5 gene pyrH or Rv2883c
-
2.7.4.22 Mycobacterium tuberculosis H37Rv P9WHK5 gene pyrH or Rv2883c
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.7.4.22 ATP + UMP
-
 Mycobacterium tuberculosis ADP + UDP
-
 r
2.7.4.22 ATP + UMP
-
 Mycobacterium tuberculosis H37Rv ADP + UDP
-
 r

Synonyms

EC Number Synonyms Comment Organism
2.7.4.22 UMPK
-
 Mycobacterium tuberculosis
2.7.4.22 uridine monophosphate kinase
-
 Mycobacterium tuberculosis

Cofactor

EC Number Cofactor Comment Organism Structure
2.7.4.22 ADP
-
 Mycobacterium tuberculosis
2.7.4.22 ATP
-
 Mycobacterium tuberculosis

General Information

EC Number General Information Comment Organism
2.7.4.22 evolution the sequence motif Gly76-Gly77-Gly78-Asn79 is specific for bacterial UMPKs and most of the conserved sequences are not present in the eukaryotic UMP/UMP-CMP kinases Mycobacterium tuberculosis
2.7.4.22 additional information homology modeling of Mtb-UMPK on the basis of the crystal structure of Escherichia coli-UMPK, structure-function relationships, molecular dynamics study, active-site modeling of the Mtb-UMPK, overview. Six lead molecules make strong hydrogen bonding interactions with Lys36, Gly39, Gly77, Gly78, Asp97, Ser164, and Thr165 amino acid residues in Mtb-UMPK model Mycobacterium tuberculosis
2.7.4.22 physiological function the allosteric regulation mechanism of the enzyme maintains the balance between synthesis of purine and pyrimidine nucleoside triphosphates Mycobacterium tuberculosis