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MGP005018

UniProt Annotations

Entry Information
Gene Namepyrroline-5-carboxylate reductase family, member 2
Protein EntryP5CR2_HUMAN
UniProt IDQ96C36
SpeciesHuman
Comments
Comment typeDescription
Biophysicochemical PropertiesKinetic parameters: KM=0.64 mM for NADH {ECO:0000269|PubMed:2722838}; KM=0.04 mM for NADPH {ECO:0000269|PubMed:2722838}; KM=1.49 mM for pyrroline-5-carboxylate (in the presence of NADH) {ECO:0000269|PubMed:2722838}; KM=0.23 mM for pyrroline-5-carboxylate (in the presence of NADPH) {ECO:0000269|PubMed:2722838}; Vmax=28.5 umol/min/ug enzyme (in the presence of NADH) {ECO:0000269|PubMed:2722838}; Vmax=3.7 umol/min/ug enzyme (in the presence of NADPH) {ECO:0000269|PubMed:2722838};
Catalytic ActivityL-proline + NAD(P)(+) = 1-pyrroline-5- carboxylate + NAD(P)H. {ECO:0000269|PubMed:2722838, ECO:0000269|PubMed:6894153}.
Enzyme RegulationSubject to competitive inhibition by NADP. Not inhibited by proline. {ECO:0000269|PubMed:2722838, ECO:0000269|PubMed:6894153}.
FunctionHousekeeping enzyme that catalyzes the last step in proline biosynthesis. In some cell types, such as erythrocytes, its primary function may be the generation of NADP(+). Can utilize both NAD and NADP. Has higher affinity for NADP, but higher catalytic efficiency with NADH. {ECO:0000269|PubMed:2722838, ECO:0000269|PubMed:6894153}.
PathwayAmino-acid biosynthesis; L-proline biosynthesis; L- proline from L-glutamate 5-semialdehyde: step 1/1.
SimilarityBelongs to the pyrroline-5-carboxylate reductase family. {ECO:0000305}.
Subcellular LocationCytoplasm {ECO:0000269|PubMed:2722838}.
SubunitHomodecamer; composed of 5 homodimers. {ECO:0000305|PubMed:2722838}.
Tissue SpecificityDetected in erythrocytes (at protein level). {ECO:0000269|PubMed:2722838, ECO:0000269|PubMed:6894153}.
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