MGP Database

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MGP005651

UniProt Annotations

Entry Information
Gene Namecarnosine synthase 1
Protein EntryCRNS1_HUMAN
UniProt IDA5YM72
SpeciesHuman
Comments
Comment typeDescription
Alternative ProductsEvent=Alternative splicing; Named isoforms=5; Name=1; IsoId=A5YM72-1; Sequence=Displayed; Name=2; IsoId=A5YM72-2; Sequence=VSP_032925; Name=3; IsoId=A5YM72-3; Sequence=VSP_032926; Note=No experimental confirmation available.; Name=4; IsoId=A5YM72-4; Sequence=VSP_053735, VSP_053736; Note=No experimental confirmation available. Ref.3 (BAG57387) sequence is in conflict in positions: 2:L->F, 395:A->V. {ECO:0000305}; Name=5; IsoId=A5YM72-5; Sequence=VSP_053735; Note=No experimental confirmation available.;
Biophysicochemical PropertiesKinetic parameters: KM=0.09 mM for beta-alanine {ECO:0000269|PubMed:20097752}; KM=1.84 mM for gamma-aminobutyrate {ECO:0000269|PubMed:20097752}; KM=0.37 mM for L-histidine {ECO:0000269|PubMed:20097752}; KM=4.67 mM for L-lysine {ECO:0000269|PubMed:20097752}; KM=7.66 mM for L-ornithine {ECO:0000269|PubMed:20097752}; KM=24.7 mM for N-methylhistidine {ECO:0000269|PubMed:20097752}; Vmax=65.3 nmol/min/mg enzyme toward beta-alanine {ECO:0000269|PubMed:20097752}; Vmax=54.7 nmol/min/mg enzyme toward gamma-aminobutyrate {ECO:0000269|PubMed:20097752}; Vmax=0.76 nmol/min/mg enzyme toward L-histidine {ECO:0000269|PubMed:20097752}; Vmax=0.61 nmol/min/mg enzyme toward L-lysine {ECO:0000269|PubMed:20097752}; Vmax=0.28 nmol/min/mg enzyme toward L-ornithine {ECO:0000269|PubMed:20097752}; Vmax=0.62 nmol/min/mg enzyme toward N-methylhistidine {ECO:0000269|PubMed:20097752};
Catalytic ActivityATP + L-histidine + beta-alanine = ADP + phosphate + carnosine.
CofactorName=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250}; Note=Binds 2 manganese ions per subunit. {ECO:0000250};
FunctionCatalyzes the synthesis of carnosine and homocarnosine. Carnosine is synthesized more efficiently than homocarnosine. {ECO:0000269|PubMed:20097752}.
Sequence CautionSequence=ABQ59056.1; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305}; Sequence=BAA92632.1; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
SimilarityContains 1 ATP-grasp domain. {ECO:0000255|PROSITE- ProRule:PRU00409}.
SubunitHomotetramer. {ECO:0000250}.
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