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Search The CSA
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Catalytic Site Atlas

CSA LITERATURE entry for 1auw

E.C. nameargininosuccinate lyase
SpeciesAnas platyrhynchos (Anas boschas)
E.C. Number (IntEnz) 4.3.2.1
CSA Homologues of 1auwThere are 46 Homologs
CSA Entries With UniProtID P24058
CSA Entries With EC Number 4.3.2.1
PDBe Entry 1auw
PDBSum Entry 1auw
MACiE Entry 1auw

Literature Report

IntroductionArgininosuccinate lyase (ASL), the enzyme homologue of delta-crystallin, is ubiquitous in all organisms, where it is involved in the biosynthesis of arginine. It catalyses the conversion of L-argininosuccinate to arginine and fumarate.
MechansimThe enzyme catalyses a beta-elimination reaction through a general acid/base mechanism. A histidine residue abstracts a proton from the substrate, forming a carbanion intermediate. Redistribution of negative charge into the carboxyl group generates the aci-carboxylate intermediate. The aci-acid or carbanion intermediates provide the driving force for the expulsion of the fumarate group. The general acid helps the final C-N bond cleavage by donating a proton to the substrate.
Reaction

Catalytic Sites for 1auw

Annotated By Reference To The Literature - Site 1 (Perform Site Search)
ResidueChainNumberUniProtKB NumberFunctional PartFunctionTargetDescription
LysA287289macie:sideChainNeutralises the negative charge on the carbanion intermediate.
GluA294296macie:sideChainActs as a general acid to promote substrate cleavage. Also increases the nucleophilicity of His160.
HisC160162macie:sideChainActs as general base to abstract a proton from C-9 of the substrate.

Literature References

Notes:
Abu-Abed M
Structural comparison of the enzymatically active and inactive forms of delta crystallin and the role of histidine 91.
Biochemistry 1997 36 14012-14022
PubMed: 9369472
Wu CY
Chemical mechanism of the endogenous argininosuccinate lyase activity of duck lens delta2-crystallin.
Biochem J 1998 333 ( Pt 2) 327-334
PubMed: 9657972
Vallée F
Crystal structure of an inactive duck delta II crystallin mutant with bound argininosuccinate.
Biochemistry 1999 38 2425-2434
PubMed: 10029536
Chakraborty AR
Mutational analysis of amino acid residues involved in argininosuccinate lyase activity in duck delta II crystallin.
Biochemistry 1999 38 2435-2443
PubMed: 10029537
Sampaleanu LM
Mutational analysis of duck delta 2 crystallin and the structure of an inactive mutant with bound substrate provide insight into the enzymatic mechanism of argininosuccinate lyase.
J Biol Chem 2002 277 4166-4175
PubMed: 11698398
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