2.7.4.22: UMP kinase
This is an abbreviated version!
For detailed information about UMP kinase, go to the full flat file.
Reaction
Synonyms
ATP:UMP phosphotransferase, HP0777 protein, More, pyrH, Rv2883c, SsUMPK, UMP kinase, UMP-kinase, UMPK, UMPKs, uridine monophosphate kinase, uridylate kinase, XC1936
ECTree
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General Information
General Information on EC 2.7.4.22 - UMP kinase
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evolution
physiological function
additional information
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
evolution
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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
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the allosteric regulation mechanism of the enzyme maintains the balance between synthesis of purine and pyrimidine nucleoside triphosphates
physiological function
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UMP kinase is an essential enzyme found only in bacteria
physiological function
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UMP kinase is an essential enzyme found only in bacteria
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physiological function
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the allosteric regulation mechanism of the enzyme maintains the balance between synthesis of purine and pyrimidine nucleoside triphosphates
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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
additional information
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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
additional information
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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
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