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Overview for MACiE Entry M0049

Version history

General Information

EC Number: 4.1.1.22 (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
  • 3.50.20.10 - Pyruvoyl-Dependent Histidine Decarboxylase, subunit B
  • Unassigned Domain

Display structure information

Overall Reaction:

Image of proton

Image of histidine

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Image of carbon dioxide

Image of histamine

proton
C00080
CHEBI:24636
histidine
C00135
CHEBI:32526
carbon dioxide
C00011
CHEBI:16526
histamine
C00388
CHEBI:18295

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 1The 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 2Tyr62 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 3The intermediate undergoes decarboxylation, with double bond rearrangement in which the pyruvoyl moiety acts as an electron sink.
Step 4The oxyanion formed initiates double bond rearrangement that results in the deprotonation of Glu197F at the CA position of the covalently attached histamine.
Step 5The C-terminal serine residue deprotonates water, which in turn attacks the imine carbon in a nucleophilic addition, the nitrogen deprotonates Tyr62.
Step 6Tyr62 deprotonates the hydroxyl group of the pyruvoyl residue, which eliminated the histamine substrate with concomitant deprotonation of the C-terminal residue.
Step 7Glu197F deprotonates water in an inferred step.

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Catalytic Residues Involved

Type Number Chain Location of Function
Tyr 62 A Side Chain
Glu 66 A Side Chain
Ser 81 E Main Chain C Terminus
Phe 195 F Main Chain Amide
Glu 197 F Side Chain
Pvl 82 F Post-translationally modified residue

References

  1. T. Gallagher et al. (1989), J. Biol. Chem., 264, 12737-12743. Pyruvoyl-dependent histidine decarboxylase. Active site structure and mechanistic analysis.
    Medline: 2745463
  2. E. J. Pishko et al. (1993), Biochemistry, 32, 4943-4948. Site-directed alteration of three active-site residues of a pyruvoyl-dependent histidine decarboxylase.
    Medline: 8490030
  3. P. D. van Poelje et al. (1990), Annu. Rev. Biochem., 59, 29-59. Pyruvoyl-dependent enzymes.
    Medline: 2197977

Homologue information for M0049 (1pya)

CSA Homologues

MACiE Homologues (within the PDB)

MACiE Homologues (within UniprotKB/SwissProt)


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
histidine decarboxylase activity (molecular function)
cellular amino acid metabolic process (biological process)
histidine metabolic process (biological process)
lyase activity (molecular function)
carboxy-lyase activity (molecular function)
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