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Search The CSA
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Catalytic Site Atlas

CSA LITERATURE entry for 1eb6

E.C. namedeuterolysin
SpeciesAspergillus oryzae (strain ATCC 42149 / RIB 40)
E.C. Number (IntEnz) 3.4.24.39
CSA Homologues of 1eb61g12,1ge5,1ge6,1ge7,
CSA Entries With UniProtID P46076
CSA Entries With EC Number 3.4.24.39
PDBe Entry 1eb6
PDBSum Entry 1eb6
MACiE Entry 1eb6

Literature Report

IntroductionDeuterolysin is a zinc metalloproteinase, part of a novel family of zinc metalloproteinases which have an Asp residue as the third zinc binding ligand in addition to the general sequence HEXXH found in all zinc metalloproteinases. It shows a preference for basic protein substrates such as histones, and is of particular importance in the Japanese fermentation industry.
MechansimGlu 129 and Zn together act to activate a water molecule so that it can act as a nucleophile to attack the peptide substrate. This forms a tetrahedral intermediate, stabilised by proton donation by Tyr 106, which then collapses to release the products.
Reaction

Catalytic Sites for 1eb6

Annotated By Reference To The Literature - Site 1 (Perform Site Search)
ResidueChainNumberUniProtKB NumberFunctional PartFunctionTargetDescription
TyrA106281macie:sideChainDonates proton to the oxyanion of the tetrahedral intermediate to stabilise the transition state.
GluA129304macie:sideChainAccepts a proton from water to activate it for nucleophilic attack on the peptide substrate, forming the tetrahedral intermediate.

Literature References

Notes:Role of Asp 143 is unclear as may be catalytic or involved in Zinc binding.
Fushimi N
Aspzincin, a family of metalloendopeptidases with a new zinc-binding motif. Identification of new zinc-binding sites (His(128), His(132), and Asp(164)) and three catalytically crucial residues (Glu(129), Asp(143), and Tyr(106)) of deuterolysin from Aspergillus oryzae by site-directed mutagenesis.
J Biol Chem 1999 274 24195-24201
PubMed: 10446194
McAuley KE
A quick solution: ab initio structure determination of a 19 kDa metalloproteinase using ACORN.
Acta Crystallogr D Biol Crystallogr 2001 57 1571-1578
PubMed: 11679721
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