spacer

Overview for MACiE Entry M0305

Version history

General Information

EC Number: 4.1.3.38 (A member of the Lyases, Carbon-carbon lyases, Oxo-acid-lyases)

Enzyme Name: aminodeoxychorismate lyase

Biological Species: Escherichia coli (Bacteria)

Catalytic Chain UniprotKB Accession Codes:

  • P28305 - Aminodeoxychorismate lyase

Representative PDB Code: 1et0 - CRYSTAL STRUCTURE OF AMINODEOXYCHORISMATE LYASE FROM ESCHERICHIA COLI (Resolution = 2.20 Å).

Catalytic CATH Codes:

  • 3.30.470.10 - D-amino Acid Aminotransferase; Chain A, domain 1
  • 3.20.10.10 - D-amino Acid Aminotransferase, subunit A, domain 2

Display structure information

Overall Reaction:

Image of 4-amino-4-deoxychorismate

right arrow

Image of 4-aminobenzoate

Image of pyruvate

4-amino-4-deoxychorismate
C11355
CHEBI:35181
4-aminobenzoate
C00568
CHEBI:17836
pyruvate
C00022
CHEBI:15361

View similar reactions


Stepwise Description of the Reaction

Step 1The amine of the substrate attacks the PLP cofactor in a nucleophilic addition and the bound Lys159 deprotonates the newly attached amine.
Step 2The secondary amine initiates an elimination of the covalently bound lysine, forming free PLP and lysine in a neutral state.
Step 3Lys159 deprotonates the CH adjacent to the bound amine, resulting in double bond rearrangement with the PLP cofactor acting as an electron sink.
Step 4The PLP feeds the electrons back, resulting in the cleavage of the C-O attached to the aromatic ring and the C=C of the released substrate deprotonating Lys159.
Step 5The amine of Lys159 attacks the PLP in a nucleophilic addition reaction, the secondary amine of the attached substrate reprotonates from the bound Lys159.
Step 6The secondary amine that results from the initial attack initiates an elimination of the covalently bound product, resulting in 4-aminobenzoate and the regenerated PLP cofactor

View similar reactions (composite manual annotation)


Catalytic Residues Involved

Type Number Chain Location of Function
Thr 38 A Side Chain
Lys 159 A Side Chain
Glu 193 A Side Chain

Organic Cofactors for M0305

Type Identity Chain
Pyridoxal 5'-phosphate PLP 413 A Overview

References

  1. T. Nakai et al. (2000), J. Biochem. (Toyko), 128, 29-38. Three-dimensional structure of 4-amino-4-deoxychorismate lyase from Escherichia coli.
    Medline: 10876155

Homologue information for M0305 (1et0)

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
M0066 D-alanine transaminase
2.6.1.21
1daa 3.30.470.10
3.20.10.10
0.78780.3985Compare

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

GOA logo
catalytic activity (molecular function)
metabolic process (biological process)
4-amino-4-deoxychorismate lyase activity (molecular function)
pyridoxal phosphate binding (molecular function)
folic acid biosynthetic process (biological process)
spacer
spacer