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Enzymes

UniProtKB

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Name ^help_outline L-alanine Identifier CHEBI:57972 Charge 0 Formula C3H7NO2 InChIKey^help_outline QNAYBMKLOCPYGJ-REOHCLBHSA-N SMILES^help_outline C[C@H]([NH3+])C([O-])=O 2D coordinates Mol file for the small molecule Search links Involved in 112 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 InChIKey^help_outline BAWFJGJZGIEFAR-NNYOXOHSSA-M SMILES^help_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 1,190 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
Name ^help_outline H₂O Identifier CHEBI:15377 (CAS: 7732-18-5) ^help_outline Charge 0 Formula H2O InChIKey^help_outline XLYOFNOQVPJJNP-UHFFFAOYSA-N SMILES^help_outline [H]O[H] 2D coordinates Mol file for the small molecule Search links Involved in 6,264 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
Name ^help_outline pyruvate Identifier CHEBI:15361 (CAS: 57-60-3) ^help_outline Charge -1 Formula C3H3O3 InChIKey^help_outline LCTONWCANYUPML-UHFFFAOYSA-M SMILES^help_outline CC(=O)C([O-])=O 2D coordinates Mol file for the small molecule Search links Involved in 215 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
Name ^help_outline NH₄⁺ Identifier CHEBI:28938 (CAS: 14798-03-9) ^help_outline Charge 1 Formula H4N InChIKey^help_outline QGZKDVFQNNGYKY-UHFFFAOYSA-O SMILES^help_outline [H][N+]([H])([H])[H] 2D coordinates Mol file for the small molecule Search links Involved in 529 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 InChIKey^help_outline BOPGDPNILDQYTO-NNYOXOHSSA-L SMILES^help_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 1,120 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 InChIKey^help_outline GPRLSGONYQIRFK-UHFFFAOYSA-N SMILES^help_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:18405	RHEA:18406	RHEA:18407	RHEA:18408
Reaction direction	undefined	left-to-right	right-to-left	bidirectional
UniProtKB ^help_outline	21,967 proteins	4 proteins	2 proteins
EC numbers ^help_outline	1.4.1.1
Gene Ontology ^help_outline	GO:0000286
KEGG ^help_outline				R00396
MetaCyc ^help_outline				ALANINE-DEHYDROGENASE-RXN
M-CSA ^help_outline		M0067

Related reactions ^help_outline

More general form(s) of this reaction

RHEA:10398
a 2-oxocarboxylate + NH₄⁺ + NADH + H⁺ => an L-α-amino acid + NAD⁺ + H₂O

Publications

Analysis of the structure and substrate binding of Phormidium lapideum alanine dehydrogenase.

Baker P.J., Sawa Y., Shibata H., Sedelnikova S.E., Rice D.W.

The structure of the hexameric L-alanine dehydrogenase from Phormidium lapideum reveals that the subunit is constructed from two domains, each having the common dinucleotide binding fold. Despite there being no sequence similarity, the fold of alanine dehydrogenase is closely related to that of th ... >> More

The structure of the hexameric L-alanine dehydrogenase from Phormidium lapideum reveals that the subunit is constructed from two domains, each having the common dinucleotide binding fold. Despite there being no sequence similarity, the fold of alanine dehydrogenase is closely related to that of the family of D-2-hydroxyacid dehydrogenases, with a similar location of the active site, suggesting that these enzymes are related by divergent evolution. L-alanine dehydrogenase and the 2-hydroxyacid dehydrogenases also use equivalent functional groups to promote substrate recognition and catalysis. However, they are arranged differently on the enzyme surface, which has the effect of directing opposite faces of the keto acid to the dinucleotide in each case, forcing a change in absolute configuration of the product. << Less

Nat Struct Biol 5:561-567(1998) [PubMed] [EuropePMC]

Comments

Published in: Itoh, N., Yachi, C. and Kudome, T. Determining a novel NAD+-dependent amine dehydrogenase with a broad substrate range from Streptomyces virginiae IFO 12827: purification and characterization. Journal of Molecular Catalysis B: Enzymatic 10 (2000) 281–290. DOI:10.1016/S1381-1177(00)00111-9

RHEA:18407 pyruvate + NH4(+) + NADH + H(+) => L-alanine + NAD(+) + H2O Reaction with net flow from right to left. help_outline