| Description | Gamma-glutamyl phosphate reductase (GPR), also known as glutamate-5-semialdehyde dehydrogenase, catalyses the second step of proline biosynthesis, the NADPH-dependent reversible reduction of gamma-glutamyl phosphate to glutamate-5-semialdehyde as shown below.L-glutamyl 5-phosphate + NADPH + H(+) = L-glutamate 5-semialdehyde + phosphate + NADP(+)In bacteria and yeast, GPR is a monofunctional protein, while in plants and mammals, it is part of a bifunctional enzyme that consists of two domains, an N-terminal glutamate 5-kinase domain ( ) and a C-terminal GPR domain [ , , ].This entry represents the monofunctional gamma-glutamyl phosphate reductase found in bacteria and yeasts. Structural studies indicate that this protein is composed of three domains and belongs to the aldehyde dehydrogenase structural family [ ]. The first two domains, the catalytic and cofactor binding domains respectively, both form a similar three layered α-β-α fold, and are thought to close around the NADPH and gamma-glutamyl-phosphate ligands upon binding in order to orient a conserved cysteine residue for catalysis. The third domain is the oligomerisation domain which forms an antiparallel β sheet. The biological oligomerisation state of the protein is not currently known, but like most members of the aldehyde dehydrogenase family it is expected to be either a dimer or a tetramer. | Name | Glutamate-5-semialdehyde dehydrogenase |
| Short Name | Glu-5-SA_DH | Type | Family |
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