spacer

Overview for MACiE Entry M0314

Version history

General Information

EC Number: 4.1.3.27 (A member of the Lyases, Carbon-carbon lyases, Oxo-acid-lyases)

Enzyme Name: anthranilate synthase

Biological Species: Sulfolobus solfataricus (Bacteria)

Catalytic Chain UniprotKB Accession Codes:

  • Q06128 - Anthranilate synthase component 1
  • Q06129 - Anthranilate synthase component II

Representative PDB Code: 1qdl - THE CRYSTAL STRUCTURE OF ANTHRANILATE SYNTHASE FROMSULFOLOBUS SOLFATARICUS (Resolution = 2.50 Å).

Catalytic CATH Codes:

Display structure information

Overall Reaction:

Image of chorismate

Image of L-glutamine

right arrow

Image of L-glutamatmic acid

Image of anthranilate

Image of pyruvate

chorismate
C00251
CHEBI:29748
L-glutamine
C00064
CHEBI:58359
L-glutamatmic acid
C00025
CHEBI:16015
anthranilate
C00108
CHEBI:16567
pyruvate
C00022
CHEBI:15361

View similar reactions


Stepwise Description of the Reaction

Step 1His170 deprotonates Cys85, activating it for a nucleophilic attack upon L-glutamine, forming an enzyme-substrate covalent bond.
Step 2The tetrahedral intermediate collapses, liberating ammonia, which deprotonates His170 and then passes to the other catalytic domain.
Step 3His170 deprotonates a water molecule, which initiates a nucleophilic attack on the Cys-bound intermediate.
Step 4The tetrahedral intermediate collapses, liberating Cys85, which deprotonates His170, and the glutamate product.
Step 5Ammiona acts as a nucleophile, adding to chorismate and eliminating water.
Step 6His398 deprotonates the C2 of the intermediate, eliminating the anthranilate product with concomitant deprotonation of the His398.

View similar reactions (composite manual annotation)


Catalytic Residues Involved

Type Number Chain Location of Function
Gly 58 B Main Chain Amide
Leu 86 B Main Chain Amide
Cys 85 B Side Chain
His 170 B Side Chain
Glu 172 B Side Chain
His 398 A Side Chain
Thr 329 A Side Chain
Arg 469 A Side Chain
Tyr 449 A Side Chain
Gly 483 A Main Chain Amide

Metal Cofactors for M0314

Type Het group Number Chain
magnesium No Available PDB Information

References

  1. G. Spraggon et al. (2001), Proc. Natl Acad. Sci. USA, 98, 6021-6026. The structures of anthranilate synthase of Serratia marcescens crystallized in the presence of (i) its substrates, chorismate and glutamine, and a product, glutamate, and (ii) its end-product inhibitor, L-tryptophan.
    Medline: 11371633
  2. T. Knöchel et al. (1999), Proc. Natl Acad. Sci. USA, 96, 9479-9484. The crystal structure of anthranilate synthase from Sulfolobus solfataricus: functional implications.
    Medline: 10449718
  3. A. A. Morollo et al. (2001), Nat. Struct. Biol., 8, 243-247. Structure of the cooperative allosteric anthranilate synthase from Salmonella typhimurium.
    Medline: 11224570

Homologue information for M0314 (1qdl)

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
M0283 aminodeoxychorismate synthase
2.6.1.85
1k0g 3.60.120.10
0.66660.2812Compare
M0234 GMP synthase (glutamine-hydrolysing)
6.3.5.2
1gpm 3.40.50.880
0.55120.45Compare

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
tryptophan biosynthetic process (biological process)
catalytic activity (molecular function)
anthranilate synthase activity (molecular function)
protein binding (molecular function)
glutamine metabolic process (biological process)
metabolic process (biological process)
cellular amino acid biosynthetic process (biological process)
biosynthetic process (biological process)
aromatic amino acid family biosynthetic process (biological process)
lyase activity (molecular function)
oxo-acid-lyase activity (molecular function)
spacer
spacer