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Overview for MACiE Entry M0199

Version history

General Information

EC Number: 6.3.2.3 (A member of the Ligases, Forming carbon-nitrogen bonds, Acid—amino-acid ligases (peptide synthases))

Enzyme Name: glutathione synthase

Biological Species: Escherichia coli (Bacteria)

Catalytic Chain UniprotKB Accession Codes:

  • P04425 - Glutathione synthetase

Representative PDB Code: 1gsa - STRUCTURE OF GLUTATHIONE SYNTHETASE COMPLEXED WITH ADP AND GLUTATHIONE (Resolution = 2.00 Å).

Catalytic CATH Codes:

"Other" CATH Codes:

Display structure information

Overall Reaction:

Image of ATP

Image of gamma-L-glutamyl-L-cysteine

Image of glycine

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Image of phosphate

Image of ADP

Image of glutathione

ATP
C00002
CHEBI:30616
gamma-L-glutamyl-L-cysteine
C00669
CHEBI:17515
glycine
C00037
CHEBI:32508
phosphate
C00009
CHEBI:18367
ADP
C00008
CHEBI:456216
glutathione
C00051
CHEBI:16856

View similar reactions


Stepwise Description of the Reaction

Step 1The carboxylate group of gamma-L-glutamyl-L-cysteine acts as a nucleophile and attacks the alpha-phoposphate of ATP in a substitution reaction, liberating ADP. The two Mg(II) ions, Lys160, Arg210 and Arg225 all stabilise the intermediates formed.
Step 2The amine group of L-glycine acts as a nucleophile and attacks the carbonyl group of the phosphorylated substrate in an addition reaction. The two Mg(II) ions, Lys160, Arg210 and Arg225 all stabilise the intermediates formed.
Step 3The oxyanion formed re-forms the carbonyl group, cleaving the P-O bond in a conjugate base elimination reaction. The leaving phosphate group deprotonates the newly formed secondary amine. The two Mg(II) ions, Lys160, Arg210 and Arg225 all stabilise the intermediates formed.

View similar reactions (composite manual annotation)


Catalytic Residues Involved

Type Number Chain Location of Function
Lys 160 A Side Chain
Arg 210 A Side Chain
Arg 225 A Side Chain

Metal Cofactors for M0199

Type Het group Number Chain
magnesium MG 319 x Overview
magnesium MG 320 x Overview

References

  1. T. Hara et al. (1996), Biochemistry, 35, 11967-11974. A pseudo-michaelis quaternary complex in the reverse reaction of a ligase: structure of Escherichia coli B glutathione synthetase complexed with ADP, glutathione, and sulfate at 2.0 A resolution.
    Medline: 8810901

Homologue information for M0199 (1gsa)

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
M0207 pyruvate, phosphate dikinase
2.7.9.1
1kc7 3.30.1490.20
3.30.470.20
0.17070.4090Compare
M0310 D-alanine-(R)-lactate ligase
6.1.2.1
1e4e 3.30.470.20
3.40.50.20
3.30.1490.20
0.33330.225Compare

View a comparison of the other reactions in MACiE with the CATH domain 3.30.1490.20

View a comparison of the other reactions in MACiE with the CATH domain 3.30.470.20

View a comparison of the other reactions in MACiE with the CATH domain 3.40.50.20


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
catalytic activity (molecular function)
glutathione synthase activity (molecular function)
ATP binding (molecular function)
glutathione biosynthetic process (biological process)
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