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Overview for MACiE Entry M0029

Version history

General Information

EC Number: 3.5.1.38 (A member of the Hydrolases, Acting on carbon-nitrogen bonds, other than peptide bonds, In linear amides)

Enzyme Name: glutamin-(asparagin-)ase

Biological Species: Pseudomonas sp. (Bacteria)

Catalytic Chain UniprotKB Accession Codes:

  • P10182 - Glutaminase-asparaginase

Representative PDB Code: 1djo - CRYSTAL STRUCTURE OF PSEUDOMONAS 7A GLUTAMINASE-ASPARAGINASE WITH THE INHIBITOR DONV COVALENTLY BOUND IN THE ACTIVE SITE (Resolution = 2.00 Å).

Catalytic CATH Codes:

Display structure information

Overall Reaction:

Image of L-asparagine

Image of water

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Image of ammonia

Image of L-aspartate

L-asparagine
C00152
CHEBI:58048
water
C00001
CHEBI:15377
ammonia
C00014
CHEBI:16134
L-aspartate
C00049
CHEBI:17053

Overall Comment: Thr-Tyr-Glu and Asp-Lys-Thr triads present.


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Stepwise Description of the Reaction

Step 1Glu3294B deprotonates Tyr1034, which in turn deprotonates Thr1020. Thr1020 then initiates a nucleophilic attack upon the amide carbon of L-asparagine in an addition reaction. The oxyanion formed deprotonates Glu3294B.
Step 2Glu3294B deprotonates the hydroxyl formed from the oxyanion, initiating the elimination of ammonia, which gains a proton from Glu3294B.
Step 3The Asp-Lys-Thr triad activates water, which initiates a nucleophilic attack on the carbonyl carbon of the covalently attached intermediate. The formed oxyanion deprotonates the water which attacked.
Step 4Glu3294B deprotonates the hydroxyl formed from the oxyanion, initiating the elimination of Thr1020, which in turn deprotonates Tyr1034, which then deprotonates Glu3294B.

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Catalytic Residues Involved

Type Number Chain Location of Function
Thr 1020 A Side Chain
Tyr 1034 A Side Chain
Thr 1100 A Side Chain
Asp 1101 A Side Chain
Lys 1173 A Side Chain
Glu 3294 B Side Chain

References

  1. E. Ortlund et al. (2000), Biochemistry, 39, 1199-1204. Reactions of Pseudomonas 7A glutaminase-asparaginase with diazo analogues of glutamine and asparagine result in unexpected covalent inhibitions and suggests an unusual catalytic triad Thr-Tyr-Glu.
    Medline: 10684596

Homologue information for M0029 (1djo)

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
asparaginase activity (molecular function)
cellular amino acid metabolic process (biological process)
asparagine metabolic process (biological process)
hydrolase activity (molecular function)
periplasmic space (cellular component)
glutamin-(asparagin-)ase activity (molecular function)
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