Enzymes
| UniProtKB help_outline | 4 proteins |
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- Name help_outline H2O Identifier CHEBI:15377 (Beilstein: 3587155; CAS: 7732-18-5) help_outline Charge 0 Formula H2O InChIKeyhelp_outline XLYOFNOQVPJJNP-UHFFFAOYSA-N SMILEShelp_outline [H]O[H] 2D coordinates Mol file for the small molecule Search links Involved in 6,204 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline L-saccharopine Identifier CHEBI:57951 Charge -1 Formula C11H19N2O6 InChIKeyhelp_outline ZDGJAHTZVHVLOT-YUMQZZPRSA-M SMILEShelp_outline [NH3+][C@@H](CCCC[NH2+][C@@H](CCC([O-])=O)C([O-])=O)C([O-])=O 2D coordinates Mol file for the small molecule Search links Involved in 5 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline NAD+ Identifier CHEBI:57540 (Beilstein: 3868403) help_outline Charge -1 Formula C21H26N7O14P2 InChIKeyhelp_outline BAWFJGJZGIEFAR-NNYOXOHSSA-M 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](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 1,186 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline (S)-2-amino-6-oxohexanoate Identifier CHEBI:58321 Charge 0 Formula C6H11NO3 InChIKeyhelp_outline GFXYTQPNNXGICT-YFKPBYRVSA-N SMILEShelp_outline [H]C(=O)CCC[C@H]([NH3+])C([O-])=O 2D coordinates Mol file for the small molecule Search links Involved in 17 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 9,431 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline L-glutamate Identifier CHEBI:29985 (CAS: 11070-68-1) help_outline Charge -1 Formula C5H8NO4 InChIKeyhelp_outline WHUUTDBJXJRKMK-VKHMYHEASA-M SMILEShelp_outline [NH3+][C@@H](CCC([O-])=O)C([O-])=O 2D coordinates Mol file for the small molecule Search links Involved in 244 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline NADH Identifier CHEBI:57945 (Beilstein: 3869564) help_outline Charge -2 Formula C21H27N7O14P2 InChIKeyhelp_outline BOPGDPNILDQYTO-NNYOXOHSSA-L 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](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 1,116 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
Cross-references
| RHEA:24520 | RHEA:24521 | RHEA:24522 | RHEA:24523 | |
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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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Familial hyperlysinemias. Purification and characterization of the bifunctional aminoadipic semialdehyde synthase with lysine-ketoglutarate reductase and saccharopine dehydrogenase activities.
Markovitz P.J., Chuang D.T., Cox R.P.
Familial hyperlysinemias are autosomal recessive disorders in the oxidative degradation of lysine. Hyperlysinemia type I is associated with a combined deficiency in lysine-ketoglutarate reductase and saccharopine dehydrogenase activities, the first two sequential steps in the lysine degradative pa ... >> More
Familial hyperlysinemias are autosomal recessive disorders in the oxidative degradation of lysine. Hyperlysinemia type I is associated with a combined deficiency in lysine-ketoglutarate reductase and saccharopine dehydrogenase activities, the first two sequential steps in the lysine degradative pathway. In familial hyperlysinemia type II, only saccharopine dehydrogenase activity is deficient. We report here that these reductase and dehydrogenase activities occur on a single protein based on the following findings. (i) The activity ratio of reductase/dehydrogenase remained constant (close to unity) throughout a 500-fold purification of both enzyme activities from mitochondrial extracts of baboon and bovine livers. The activity profiles of the reductase and the dehydrogenase superimpose on each other as the enzyme was eluted from DEAE-cellulose and Sephacryl S-300 columns. (ii) Activity-staining of the native polyacrylamide gel showed that both activities migrated the same distance toward the anode. (iii) The highly purified enzyme with the reductase and dehydrogenase activities showed a single polypeptide band of Mr = 115,000 in sodium dodecyl sulfate-polyacrylamide gel electrophoresis. The native enzyme from baboon and bovine livers has an apparent Mr of 468,000 (Stokes radius = 69.5 A) as determined by gel filtration, which suggests a tetrameric structure of identical subunits. The presence in mammalian tissues of a single protein catalyzing both the reductase and dehydrogenase reactions explains the combined enzyme deficiency observed in hyperlysinemia type I. We propose that the bifunctional enzyme be called aminoadipic semialdehyde synthase. << Less
J Biol Chem 259:11643-11646(1984) [PubMed] [EuropePMC]
This publication is cited by 1 other entry.