| Predicate | Object |
|---|---|
| rdf:type | |
| biopax3:cellularLocation | |
| biopax3:comment |
Formation of |FRAME: L-DELTA1-PYRROLINE_5-CARBOXYLATE| (or |FRAME:L-GLUTAMATE_GAMMA-SEMIALDEHYDE|, which is in nonenzymatic equilibrium with it) from glutamate in humans is catalyzed by a single bifunctional enzyme with both γ-glutamyl kinase (EC 2.7.2.11) and γ-glutamyl phosphate reductase (EC 1.2.1.41) activities |CITS:[8761662][10037775]|, as is the case in plants |CITS:[1384052]|. This is in contrast to prokaryotes and lower eukaryotes such as |FRAME: TAX-559292|, in which these two reactions are catalyzed by two different enzymes |CITS:[6933554]|. This bifunctional enzyme exists in two forms, with the longer form (HsP5CS.long) containing two more amino acids than the short form (HsP5CS.short), a result of alternative splicing |CITS:[10037775]|. The combined enzymatic activity of this enzyme has been named |FRAME: L-DELTA1-PYRROLINE_5-CARBOXYLATE| synthase, or P5CS for short. The two forms are found in many tissues, in a ratio of about 1:4 (short to long). The enzyme shows the highest expression in pancreas, ovary, testis, and kidney, followed by colon, small intestine, placenta, heart and skeletal muscle. Both forms were able to complement mutations in yeast in both functions. The short form was sensitive to inhibition by ornithine, while the long form was not |CITS:[10037775]|. The phenotypic features of deficiency of P5CS include joint hyperlaxity, skin hyperelasticity, cataract and mental retardation with hyperammonemia and low plasma levels of proline, citrulline and ornithine |CITS:[8761662][15517380]|.
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| biopax3:xref | |
| biopax3:dataSource | |
| biopax3:displayName |
GK
|
| biopax3:name |
Aldehyde dehydrogenase family 18 member A1,
GPR,
Gamma-glutamyl kinase,
Glutamate-5-semialdehyde dehydrogenase,
Glutamyl-gamma-semialdehyde dehydrogenase,
P5CS
|
| biopax3:entityReference | |
| biopax3:standardName |
Gamma-glutamyl phosphate reductase
|