Activating Compound | Comment | Organism | Structure |
---|---|---|---|
GTP | allosteric activation | Mycobacterium tuberculosis |
Application | Comment | Organism |
---|---|---|
drug development | the enzyme is a potential drug target for developing novel anti-tuberculosis drugs | Mycobacterium tuberculosis |
Cloned (Comment) | Organism |
---|---|
gene pyrH or Rv2883c, sequence comparisons and phylogenetic analysis and tree | Mycobacterium tuberculosis |
Inhibitors | Comment | Organism | Structure |
---|---|---|---|
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-(4-acetyl-3,5-dimethyl-1H-pyrazol-1-yl)-N-[1-(2-methoxybenzyl)-1H-pyrazol-5-yl]acetamide | - |
Mycobacterium tuberculosis | |
4-[2-amino-4-(4-chlorophenyl)-7-oxo-5,7-dihydro-6H-pyrrolo[3,4-d]pyrimidin-6-yl]butanoic acid | - |
Mycobacterium tuberculosis | |
4-[2-amino-4-(4-methoxyphenyl)-7-oxo-5,7-dihydro-6H-pyrrolo[3,4-d]pyrimidin-6-yl]butanoic acid | - |
Mycobacterium tuberculosis | |
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 | |
additional information | structure-based inhibitor design, inhibitor screening and molecular docking study | Mycobacterium tuberculosis | |
N-benzyl-2-[(2S,3R,4S,5R)-3,4-dihydroxy-5-[[(methylsulfonyl)amino]methyl]tetrahydrofuran-2-yl]-N-methylacetamide | - |
Mycobacterium tuberculosis | |
UTP | physiological inhibitor | Mycobacterium tuberculosis |
Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
Mg2+ | required | Mycobacterium tuberculosis |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
ATP + UMP | Mycobacterium tuberculosis | - |
ADP + UDP | - |
r | |
ATP + UMP | Mycobacterium tuberculosis H37Rv | - |
ADP + UDP | - |
r |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Mycobacterium tuberculosis | P9WHK5 | gene pyrH or Rv2883c | - |
Mycobacterium tuberculosis H37Rv | P9WHK5 | gene pyrH or Rv2883c | - |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
ATP + UMP | - |
Mycobacterium tuberculosis | ADP + UDP | - |
r | |
ATP + UMP | - |
Mycobacterium tuberculosis H37Rv | ADP + UDP | - |
r |
Synonyms | Comment | Organism |
---|---|---|
UMPK | - |
Mycobacterium tuberculosis |
uridine monophosphate kinase | - |
Mycobacterium tuberculosis |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
ADP | - |
Mycobacterium tuberculosis | |
ATP | - |
Mycobacterium tuberculosis |
General Information | Comment | Organism |
---|---|---|
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 |
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 |
physiological function | the allosteric regulation mechanism of the enzyme maintains the balance between synthesis of purine and pyrimidine nucleoside triphosphates | Mycobacterium tuberculosis |