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Search The CSA
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Catalytic Site Atlas

CSA LITERATURE entry for 2tpl

E.C. nametyrosine phenol-lyase
SpeciesCitrobacter freundii ()
E.C. Number (IntEnz) 4.1.99.2
CSA Homologues of 2tpl1c7g,1tpl,2ez1,2ez2,2vlf,2vlh,
CSA Entries With UniProtID P31013
CSA Entries With EC Number 4.1.99.2
PDBe Entry 2tpl
PDBSum Entry 2tpl
MACiE Entry 2tpl

Literature Report

Introduction
Mechansim
Reaction

Catalytic Sites for 2tpl

Annotated By Reference To The Literature - Site 3 (Perform Site Search)
ResidueChainNumberUniProtKB NumberFunctional PartFunctionTargetDescription
LlpA257257macie:ptm
TyrA7171macie:sideChain
ArgA381381macie:sideChain
PheA123123macie:sideChain
AspA214214macie:sideChain

Annotated By Reference To The Literature - Site 4 (Perform Site Search)
ResidueChainNumberUniProtKB NumberFunctional PartFunctionTargetDescription
TyrB7171macie:sideChain
ArgB381381macie:sideChain
PheB123123macie:sideChain
AspB214214macie:sideChain

Literature References

Notes:
Sundararaju B
The crystal structure of Citrobacter freundii tyrosine phenol-lyase complexed with 3-(4'-hydroxyphenyl)propionic acid, together with site-directed mutagenesis and kinetic analysis, demonstrates that arginine 381 is required for substrate specificity.
Biochemistry 1997 36 6502-6510
PubMed: 9174368
Barbolina MV
Citrobacter freundii tyrosine phenol-lyase: the role of asparagine 185 in modulating enzyme function through stabilization of a quinonoid intermediate.
Protein Eng 2000 13 207-215
PubMed: 10775663
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