Overview for MACiE Entry M0049
EC Number: 188.8.131.52 (A member of the Lyases, Carbon-carbon lyases, Carboxy-lyases)
Enzyme Name: histidine decarboxylase
Biological Species: Lactobacillus 30a (Bacteria)
Catalytic Chain UniprotKB Accession Codes:
- P00862 - Histidine decarboxylase alpha chain
Representative PDB Code: 1pya - REFINED STRUCTURE OF THE PYRUVOYL-DEPENDENT HISTIDINEDECARBOXYLASE FROM LACTOBACILLUS 30A (Resolution = 2.50 Å).
Catalytic CATH Codes:
- 4.10.510.10 - Pyruvoyl-Dependent Histidine Decarboxylas, subunit A
- 184.108.40.206 - Pyruvoyl-Dependent Histidine Decarboxylase, subunit B
- Unassigned Domain
Display structure information
Overall Comment: Pyruvoyl is covalently bound to the enzyme via main chain nitrogen of Ser82F and named Pvl82F.
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Stepwise Description of the Reaction
|Step 1||The C-terminal serine deprotonates the amine of the substrate, which attacked the terminal carbonyl carbon of the PTM pyruvoyl residue in the first step of a Schiff base formation. The oxyanion deprotonates Tyr62.|
|Step 2||Tyr62 deprotonates the newly formed secondary amine, which causes the elimination of water with concomitant deprotonation of the C-terminal serine residue, forming the Schiff base.|
|Step 3||The intermediate undergoes decarboxylation, with double bond rearrangement in which the pyruvoyl moiety acts as an electron sink.|
|Step 4||The oxyanion formed initiates double bond rearrangement that results in the deprotonation of Glu197F at the CA position of the covalently attached histamine.|
|Step 5||The C-terminal serine residue deprotonates water, which in turn attacks the imine carbon in a nucleophilic addition, the nitrogen deprotonates Tyr62.|
|Step 6||Tyr62 deprotonates the hydroxyl group of the pyruvoyl residue, which eliminated the histamine substrate with concomitant deprotonation of the C-terminal residue.|
|Step 7||Glu197F deprotonates water in an inferred step.|
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Catalytic Residues Involved
||Location of Function
||Main Chain C Terminus
||Main Chain Amide
||Post-translationally modified residue
- T. Gallagher et al. (1989), J. Biol. Chem., 264, 12737-12743. Pyruvoyl-dependent histidine decarboxylase. Active site structure and mechanistic analysis.
- E. J. Pishko et al. (1993), Biochemistry, 32, 4943-4948. Site-directed alteration of three active-site residues of a pyruvoyl-dependent histidine decarboxylase.
- P. D. van Poelje et al. (1990), Annu. Rev. Biochem., 59, 29-59. Pyruvoyl-dependent enzymes.
Homologue information for M0049 (1pya)
MACiE Homologues (within the PDB)
MACiE Homologues (within UniprotKB/SwissProt)
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