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UniProt functional annotation for Q9JHW2 | ||
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| UniProt code: Q9JHW2. |
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| Organism: | |
Mus musculus (Mouse). |
| Taxonomy: | |
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae; Murinae; Mus; Mus. |
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| Function: | |
Has omega-amidase activity (PubMed:19596042, PubMed:28373563). The role of omega-amidase is to remove potentially toxic intermediates by converting 2-oxoglutaramate and 2-oxosuccinamate to biologically useful 2-oxoglutarate and oxaloacetate, respectively (PubMed:19596042). Can also hydrolyze gamma-monomethyl-alpha- ketoglutarate in vitro (PubMed:19596042). {ECO:0000269|PubMed:19596042, ECO:0000269|PubMed:28373563}. |
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| Catalytic activity: | |
Reaction=a monoamide of a dicarboxylate + H2O = a dicarboxylate + NH4(+); Xref=Rhea:RHEA:11716, ChEBI:CHEBI:15377, ChEBI:CHEBI:28938, ChEBI:CHEBI:28965, ChEBI:CHEBI:77450; EC=3.5.1.3; Evidence={ECO:0000269|PubMed:19596042, ECO:0000269|PubMed:28373563}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:11717; Evidence={ECO:0000269|PubMed:19596042, ECO:0000269|PubMed:28373563}; |
| Catalytic activity: | |
Reaction=2-oxoglutaramate + H2O = 2-oxoglutarate + NH4(+); Xref=Rhea:RHEA:32963, ChEBI:CHEBI:15377, ChEBI:CHEBI:16769, ChEBI:CHEBI:16810, ChEBI:CHEBI:28938; EC=3.5.1.3; Evidence={ECO:0000269|PubMed:19596042, ECO:0000269|PubMed:28373563}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:32964; Evidence={ECO:0000269|PubMed:19596042, ECO:0000269|PubMed:28373563}; |
| Catalytic activity: | |
Reaction=2-oxosuccinamate + H2O = NH4(+) + oxaloacetate; Xref=Rhea:RHEA:59412, ChEBI:CHEBI:15377, ChEBI:CHEBI:16452, ChEBI:CHEBI:28938, ChEBI:CHEBI:57735; EC=3.5.1.3; Evidence={ECO:0000269|PubMed:19596042}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:59413; Evidence={ECO:0000269|PubMed:19596042}; |
| Biophysicochemical properties: | |
Kinetic parameters: KM=0.195 mM for 2-oxoglutaramate (at pH 8.5) {ECO:0000269|PubMed:19596042}; KM=0.25 mM for 2-oxoglutaramate (at pH 8.5) {ECO:0000269|PubMed:28373563}; KM=1.48 mM for glutaramate (at pH 7.2) {ECO:0000269|PubMed:19596042}; KM=1.27 mM for glutaramate (at pH 8.5) {ECO:0000269|PubMed:19596042}; KM=0.14 mM for succinamate (at pH 8.5) {ECO:0000269|PubMed:19596042}; KM=0.017 mM for 2-oxosuccinamate (at pH 8.5) {ECO:0000269|PubMed:19596042}; KM=0.003 mM for 2-oxosuccinamate (at pH 7.2) {ECO:0000269|PubMed:19596042}; KM=0.012 mM for gamma-monomethyl-alpha-ketoglutarate (at pH 7.2) {ECO:0000269|PubMed:19596042}; Vmax=32.0 umol/min/mg enzyme with 2-oxoglutaramate as substrate (at pH 8.5) {ECO:0000269|PubMed:19596042}; Vmax=19.4 umol/min/mg enzyme with 2-oxoglutaramate as substrate (at pH 8.5) {ECO:0000269|PubMed:28373563}; Vmax=1.6 umol/min/mg enzyme with 2-oxosuccinamate as substrate (at pH 8.5) {ECO:0000269|PubMed:19596042}; Vmax=16 umol/min/mg enzyme with glutaramate as substrate (at pH 8.5) {ECO:0000269|PubMed:19596042}; Vmax=5.1 umol/min/mg enzyme with succinamate as substrate (at pH 8.5) {ECO:0000269|PubMed:19596042}; Vmax=245.2 umol/min/mg enzyme with gamma-monomethyl-alpha- ketoglutarate as substrate (at pH 7.2) {ECO:0000269|PubMed:19596042}; Vmax=7.5 umol/min/mg enzyme with glutaramate as substrate (at pH 7.2) {ECO:0000269|PubMed:19596042}; Vmax=3.6 umol/min/mg enzyme with succinamate as substrate (at pH 7.2) {ECO:0000269|PubMed:19596042}; Vmax=2.1 umol/min/mg enzyme with 2-oxosuccinamate as substrate (at pH 7.2) {ECO:0000269|PubMed:19596042}; Note=In solution, 2-oxoglutaramate is in equilibrium with a cyclic form (2-hydroxy-5-oxoproline), and at pH 8.0 or above, the rate of ring opening is no longer limiting for the omega-amidase reaction (PubMed:19596042). kcat is 10.7 sec(-1) with 2-oxoglutaramate as substrate (PubMed:28373563). {ECO:0000269|PubMed:19596042, ECO:0000269|PubMed:28373563}; |
| Subunit: | |
Homodimer. {ECO:0000269|PubMed:19053248, ECO:0000305|PubMed:19595734}. |
| Subcellular location: | |
Cytoplasm {ECO:0000250|UniProtKB:Q9NQR4}. |
| Similarity: | |
Belongs to the carbon-nitrogen hydrolase superfamily. NIT1/NIT2 family. {ECO:0000305}. |
Annotations taken from UniProtKB at the EBI.