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Overview for MACiE Entry M0067

Version history

General Information

EC Number: 1.4.1.1 (A member of the Oxidoreductases, Acting on the CH-NH2 group of donors, With NAD+ or NADP+ as acceptor)

Enzyme Name: alanine dehydrogenase

Biological Species: Phormidium lapideum (Bacteria)

Catalytic Chain UniprotKB Accession Codes:

  • O52942 - Alanine dehydrogenase

Representative PDB Code: 1pjb - L-ALANINE DEHYDROGENASE (Resolution = 2.10 Å).

Catalytic CATH Codes:

Display structure information

Overall Reaction:

Image of L-alanine

Image of water

Image of NAD

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Image of ammonium

Image of NADH

Image of pyruvate

L-alanine
C00041
CHEBI:57972
water
C00001
CHEBI:15377
NAD
C00003
CHEBI:15846
ammonium
C01342
CHEBI:28938
NADH
C00004
CHEBI:16908
pyruvate
C00022
CHEBI:15361

Overall Comment: The role of Glu117 might be played by Asp269, the roles of His95 and Glu117 have been inferred from analogy to other L-2-hydroxyacid dehydrogenases as both residues are fully conserved in L-Ala DH sequences. Role of Tyr93 is tentatively assigned only. Biochemical data has suggested that the chemical mechanism proceeds through iminopyruvate and carbinolamine intermediates, with the stereochemistry of the carbinolamine thought to be that of L-amino and D-hydroxy groups [1].


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Stepwise Description of the Reaction

Step 1The amine of alanine initiates the elimination of the hydride ion, which adds to NAD.
Step 2Glu117 deprotonates His95, which undergoes double bond rearrangement and deprotonates water, which initiates a nucleophilic attack on the carbinolamine carbon in an addition reaction.
Step 3The amine deprotonates the hydroxide added, which initiates an elimination of ammoina.
Step 4Ammonia deprotonates His95, which undergoes double bond rearrangement and deprotonates Glu117 in an inferred return step.

View similar reactions (composite manual annotation)


Catalytic Residues Involved

Type Number Chain Location of Function
Lys 74 A Side Chain
Tyr 93 A Side Chain
His 95 A Side Chain
Glu 117 A Side Chain

References

  1. P. J. Baker et al. (1998), Nat. Struct. Biol., 5, 561-567. Analysis of the structure and substrate binding of Phormidium lapideum alanine dehydrogenase.
    Medline: 9665169

Homologue information for M0067 (1pjb)

CSA Homologues

MACiE Homologues (within the PDB)

MACiE Homologues (within UniprotKB/SwissProt)



Entries with at least one Catalytic CATH code in common (different mechanisms):

MACiE Entry Enzyme Name
EC Number
PDB code CATH code Composite
Reaction Similarity
Catalytic Machinery
Similarity
M0116 NAD(P)+ transhydrogenase (AB-specific)
1.6.1.2
1hzz 3.40.50.1770
0.21420.0999Compare

Links to this entry in other databases

Link to EC-PDB-SUM Link to PDB-SUM Link to RCSB PDB Link to PDBe Link to CSA
Link to MetaCyc Link to KEGG Link to BRENDA Link to ExplorENZ
Link to EzCatDB

GOA logo
nucleotide binding (molecular function)
alanine dehydrogenase activity (molecular function)
catalytic activity (molecular function)
binding (molecular function)
metabolic process (biological process)
oxidoreductase activity (molecular function)
oxidation-reduction process (biological process)
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