Enzymes
| UniProtKB help_outline | 38,849 proteins |
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- Name help_outline L-glutamate 5-semialdehyde Identifier CHEBI:58066 Charge 0 Formula C5H9NO3 InChIKeyhelp_outline KABXUUFDPUOJMW-BYPYZUCNSA-N SMILEShelp_outline [H]C(=O)CC[C@H]([NH3+])C([O-])=O 2D coordinates Mol file for the small molecule Search links Involved in 11 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline phosphate Identifier CHEBI:43474 Charge -2 Formula HO4P InChIKeyhelp_outline NBIIXXVUZAFLBC-UHFFFAOYSA-L SMILEShelp_outline OP([O-])([O-])=O 2D coordinates Mol file for the small molecule Search links Involved in 1,002 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline NADP+ Identifier CHEBI:58349 Charge -3 Formula C21H25N7O17P3 InChIKeyhelp_outline XJLXINKUBYWONI-NNYOXOHSSA-K SMILEShelp_outline NC(=O)c1ccc[n+](c1)[C@@H]1O[C@H](COP([O-])(=O)OP([O-])(=O)OC[C@H]2O[C@H]([C@H](OP([O-])([O-])=O)[C@@H]2O)n2cnc3c(N)ncnc23)[C@@H](O)[C@H]1O 2D coordinates Mol file for the small molecule Search links Involved in 1,294 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline L-glutamyl 5-phosphate Identifier CHEBI:58274 Charge -2 Formula C5H8NO7P InChIKeyhelp_outline PJRXVIJAERNUIP-VKHMYHEASA-L SMILEShelp_outline [NH3+][C@@H](CCC(=O)OP([O-])([O-])=O)C([O-])=O 2D coordinates Mol file for the small molecule Search links Involved in 2 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline NADPH Identifier CHEBI:57783 (Beilstein: 10411862) help_outline Charge -4 Formula C21H26N7O17P3 InChIKeyhelp_outline ACFIXJIJDZMPPO-NNYOXOHSSA-J SMILEShelp_outline NC(=O)C1=CN(C=CC1)[C@@H]1O[C@H](COP([O-])(=O)OP([O-])(=O)OC[C@H]2O[C@H]([C@H](OP([O-])([O-])=O)[C@@H]2O)n2cnc3c(N)ncnc23)[C@@H](O)[C@H]1O 2D coordinates Mol file for the small molecule Search links Involved in 1,288 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline H+ Identifier CHEBI:15378 Charge 1 Formula H InChIKeyhelp_outline GPRLSGONYQIRFK-UHFFFAOYSA-N SMILEShelp_outline [H+] 2D coordinates Mol file for the small molecule Search links Involved in 9,521 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
Cross-references
| RHEA:19541 | RHEA:19542 | RHEA:19543 | RHEA:19544 | |
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| Reaction direction help_outline | undefined | left-to-right | right-to-left | bidirectional |
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Publications
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Proline biosynthesis in Escherichia coli. Stoichiometry and end-product identification of the reaction catalysed by glutamate semialdehyde dehydrogenase.
Hayzer D.J., Leisinger T.
The stoichiometry of the oxidative phosphorylation of glutamic acid 5-semialdehyde by gamma-glutamyl phosphate reductase (glutamate semialdehyde dehydrogenase) has been established. Equimolar amounts of NADP+ and L-glutamic acid 5-semialdehyde are consumed and equimolar amounts of 5-oxiopyrroilidi ... >> More
The stoichiometry of the oxidative phosphorylation of glutamic acid 5-semialdehyde by gamma-glutamyl phosphate reductase (glutamate semialdehyde dehydrogenase) has been established. Equimolar amounts of NADP+ and L-glutamic acid 5-semialdehyde are consumed and equimolar amounts of 5-oxiopyrroilidine-2-carboxylic acid and NADPH are formed. The end-product of the reaction is demonstrated to be 5-oxopyrrolidine-2-carboxylic acid, probably arising from the true end-product gamma-glutamyl phosphate. << Less
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ALDH18A1 gene mutations cause dominant spastic paraplegia SPG9: loss of function effect and plausibility of a dominant negative mechanism.
Panza E., Escamilla-Honrubia J.M., Marco-Marin C., Gougeard N., De Michele G., Morra V.B., Liguori R., Salviati L., Donati M.A., Cusano R., Pippucci T., Ravazzolo R., Nemeth A.H., Smithson S., Davies S., Hurst J.A., Bordo D., Rubio V., Seri M.
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Proline biosynthesis in Escherichia coli. Purification and characterisation of glutamate-semialdehyde dehydrogenase.
Hayzer D.J., Leisinger T.
Glutamate-semialdehyde dehydrogenase, catalysing the reduction in vivo of gamma-glutamyl phosphate to glutamate 5-semialdehyde in the pathway of proline biosynthesis in Escherichia coli, has been purified to homogeneity. High initial levels of the enzyme were achieved by using a multicopy ColEl-pr ... >> More
Glutamate-semialdehyde dehydrogenase, catalysing the reduction in vivo of gamma-glutamyl phosphate to glutamate 5-semialdehyde in the pathway of proline biosynthesis in Escherichia coli, has been purified to homogeneity. High initial levels of the enzyme were achieved by using a multicopy ColEl-pro A, B hybrid plasmid. The protein has a molecular weight of 1.89 X 10(5) and consists of four identical subunits of molecular weight 4.7 X 10(4) each. The pH optimum is 7.0 and the protein is stable for at least 10 min between pH 6.0-9.0 and for long periods at pH 7.0 It is rapidly inactivated at temperatures greater than 50 degrees C. The enzyme is very sensitive to inhibition by p-chloro-mercuribenzoate, copper and nickel ions. << Less
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The biosynthesis of proline in Escherichia coli: phosphate-dependent glutamate -semialdehyde dehydrogenase (NADP), the second enzyme in the pathway.
Baich A.