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Search The CSA
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Catalytic Site Atlas

CSA LITERATURE entry for 1nlu

E.C. namesedolisin
SpeciesPseudomonas sp. (Bacteria)
E.C. Number (IntEnz) 3.4.21.100
CSA Homologues of 1nluThere are 20 Homologs
CSA Entries With UniProtID P42790
CSA Entries With EC Number 3.4.21.100
PDBe Entry 1nlu
PDBSum Entry 1nlu
MACiE Entry 1nlu

Literature Report

IntroductionSedolisins are proteolytic enzymes resembling subtilisin. They are a related family of serine-carboxyl peptidases with a unique Ser-Glu-Asp catalytic triad and require calcium ions to maintain structural integrity.
MechansimSer 287 acts as a nucleophile to attack the scissile bond and form an acyl-enzyme intermediate. Glu 80 interacts with Ser 287, and Asp 84 in turn with Glu 80. A chain of proton donors originates with a bound water molecule interacting with protonated Asp 84. In turn, this residue interacts with protonated Glu 80, which donates a proton to Ser 287. A water molecule accepts protons from Ser 287, and protonated Asp 170 which forms the oxyanion hole stabilising the tetrahedral intermediate.
Reaction

Catalytic Sites for 1nlu

Annotated By Reference To The Literature - Site 1 (Perform Site Search)
ResidueChainNumberUniProtKB NumberFunctional PartFunctionTargetDescription
GluA80295macie:sideChainInvolved in proton relay, and activates Ser 287 to allow it to act as a nucleophile in attack of the protein's scissile bond.
AspA170385macie:sideChainForms the oxyanion hole and stabilises the tetrahedral transition state.
SerA287502macie:sideChainActs as a nucleophile to attack the scissile bond in the polypeptide.
AspA84299macie:sideChainInvolved in proton transfer system and activates Glu 80.

Literature References

Notes:
Wlodawer A
Structural and enzymatic properties of the sedolisin family of serine-carboxyl peptidases.
Acta Biochim Pol 2003 50 81-102
PubMed: 12673349
Oda K
Substrate specificity and kinetic properties of pepstatin-insensitive carboxyl proteinase from Pseudomonas sp. No. 101.
Biochim Biophys Acta 1992 1120 208-214
PubMed: 1562589
Oyama H
Identification of catalytic residues of pepstatin-insensitive carboxyl proteinases from prokaryotes by site-directed mutagenesis.
J Biol Chem 1999 274 27815-27822
PubMed: 10488127
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