EzCatDB: D00231
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DB codeD00231
RLCP classification1.13.200.966 : Hydrolysis
CATH domainDomain 12.40.70.10 : Cathepsin D, subunit A; domain 1Catalytic domain
Domain 22.40.70.10 : Cathepsin D, subunit A; domain 1Catalytic domain
E.C.3.4.23.25
CSA2jxr

CATH domainRelated DB codes (homologues)
2.40.70.10 : Cathepsin D, subunit A; domain 1D00471,D00436,D00438,D00439,D00440,D00441,D00442,D00443,D00437,D00444,D00423,D00445,D00484,M00206,M00166,D00529

Enzyme Name
UniProtKBKEGG

P07267
Protein nameSaccharopepsinsaccharopepsin
yeast endopeptidase A
Saccharomyces aspartic proteinase
aspartic proteinase yscA
proteinase A
proteinase yscA
yeast proteinase A
Saccharomyces cerevisiae aspartic proteinase A
yeast proteinase A
PRA
SynonymsEC 3.4.23.25
Aspartate protease
Proteinase A
Proteinase YSCA
Carboxypeptidase Y-deficient protein 4
RefSeqNP_015171.1 (Protein)
NM_001183968.1 (DNA/RNA sequence)
MEROPSA01.018 (Aspartic)
PfamPF00026 (Asp)
[Graphical view]


UniProtKB:Accession NumberP07267
Entry nameCARP_YEAST
ActivityHydrolysis of proteins with broad specificity for peptide bonds. Cleaves -Leu-Leu-|-Val-Tyr- bond in a synthetic substrate. Does not act on esters of Tyr or Arg.
Subunit
Subcellular locationVacuole. Note=Lysosome-like vacuoles.
Cofactor

Compound table: links to PDB-related databases & PoSSuM

SubstratesProductsintermediates
KEGG-idC00017C00012C00001C00017C00012I00136
CompoundProteinPeptideH2OProteinPeptideAmino-diol-tetrahedral intermediate
Typepeptide/proteinpeptide/proteinH2Opeptide/proteinpeptide/protein
ChEBI

15377



PubChem

962
22247451



              
1dp5A01UnboundUnbound UnboundUnboundUnbound
1dpjA01UnboundUnbound UnboundUnboundUnbound
1fmuA01UnboundUnbound UnboundUnboundUnbound
1fmxA01UnboundUnbound UnboundUnboundUnbound
1fmxB01UnboundUnbound UnboundUnboundUnbound
1fq4A01UnboundAnalogue:2Y2 UnboundUnboundUnbound
1fq5A01UnboundAnalogue:0GM UnboundUnboundUnbound
1fq6A01UnboundAnalogue:0QF UnboundUnboundUnbound
1fq7A01UnboundAnalogue:2Y3 UnboundUnboundUnbound
1fq8A01UnboundAnalogue:2Y4 UnboundUnboundUnbound
1g0vA01UnboundUnbound UnboundUnboundUnbound
1jxrA01UnboundUnbound UnboundUnboundTransition-state-analogue:MOR-PHE-NLE-CHF-NME(chain I)
2jxrA01UnboundUnbound UnboundUnboundTransition-state-analogue:2Z3
1dp5A02UnboundUnbound UnboundUnboundUnbound
1dpjA02UnboundUnbound UnboundUnboundUnbound
1fmuA02UnboundUnbound UnboundUnboundUnbound
1fmxA02UnboundUnbound UnboundUnboundUnbound
1fmxB02UnboundUnbound UnboundUnboundUnbound
1fq4A02UnboundUnbound UnboundUnboundUnbound
1fq5A02UnboundUnbound UnboundUnboundUnbound
1fq6A02UnboundUnbound UnboundUnboundUnbound
1fq7A02UnboundUnbound UnboundUnboundUnbound
1fq8A02UnboundUnbound UnboundUnboundUnbound
1g0vA02UnboundUnbound UnboundUnboundUnbound
1jxrA02UnboundUnbound UnboundUnboundUnbound
2jxrA02UnboundUnbound UnboundUnboundUnbound

Active-site residues
resource
Swiss-prot;P07267
pdbCatalytic residuescomment
          
1dp5A01ASP  32
 
1dpjA01ASP  32
 
1fmuA01ASP  32
 
1fmxA01ASP  33
 
1fmxB01ASP  33
 
1fq4A01ASP  32
 
1fq5A01ASP  32
 
1fq6A01ASP  32
 
1fq7A01ASP  32
 
1fq8A01ASP  32
 
1g0vA01ASP  32
 
1jxrA01ASP  32
 
2jxrA01ASP  32
 
1dp5A02ASP 215
 
1dpjA02ASP 215
 
1fmuA02ASP 217
 
1fmxA02ASP 218
 
1fmxB02ASP 218
 
1fq4A02ASP 215
 
1fq5A02ASP 215
 
1fq6A02ASP 215
 
1fq7A02ASP 215
 
1fq8A02ASP 215
 
1g0vA02ASP 215
 
1jxrA02ASP 215
mutant L315I
2jxrA02ASP 215
mutant L315I

References for Catalytic Mechanism
ReferencesSectionsNo. of steps in catalysis
[3]


references
[1]
PubMed ID1959673
JournalFEBS Lett
Year1991
Volume293
Pages62-6
AuthorsRupp S, Hirsch HH, Wolf DH
TitleBiogenesis of the yeast vacuole (lysosome). Active site mutation in the vacuolar aspartate proteinase yscA blocks maturation of vacuolar proteinases.
[2]
PubMed ID8540315
JournalAdv Exp Med Biol
Year1995
Volume362
Pages155-66
AuthorsAguilar CF, Dhanaraj V, Guruprasad K, Dealwis C, Badasso M, Cooper JB, Wood SP, Blundell TL
TitleComparisons of the three-dimensional structures, specificities and glycosylation of renins, yeast proteinase A and cathepsin D.
[3]
CommentsX-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS)
Medline ID97280793
PubMed ID9135120
JournalJ Mol Biol
Year1997
Volume267
Pages899-915
AuthorsAguilar CF, Cronin NB, Badasso M, Dreyer T, Newman MP, Cooper JB, Hoover DJ, Wood SP, Johnson MS, Blundell TL
TitleThe three-dimensional structure at 2.4 A resolution of glycosylated proteinase A from the lysosome-like vacuole of Saccharomyces cerevisiae.
Related PDB1jxr,2jxr
Related UniProtKBP07267
[4]
CommentsX-ray crystallography
PubMed ID11061973
JournalJ Mol Biol
Year2000
Volume303
Pages745-60
AuthorsCronin NB, Badasso MO, J Tickle I, Dreyer T, Hoover DJ, Rosati RL, Humblet CC, Lunney EA, Cooper JB
TitleX-ray structures of five renin inhibitors bound to saccharopepsin: exploration of active-site specificity.
Related PDB1fq4,1fq5,1fq6,1fq7,1fq8
[5]
CommentsX-ray crystallography
PubMed ID10655612
JournalNat Struct Biol
Year2000
Volume7
Pages113-7
AuthorsLi M, Phylip LH, Lees WE, Winther JR, Dunn BM, Wlodawer A, Kay J, Gustchina A
TitleThe aspartic proteinase from Saccharomyces cerevisiae folds its own inhibitor into a helix.
Related PDB1dp5,1dpj
[6]
CommentsX-ray crystallography
PubMed ID11042188
JournalJ Biol Chem
Year2001
Volume276
Pages2023-30
AuthorsPhylip LH, Lees WE, Brownsey BG, Bur D, Dunn BM, Winther JR, Gustchina A, Li M, Copeland T, Wlodawer A, Kay J
TitleThe potency and specificity of the interaction between the IA3 inhibitor and its target aspartic proteinase from Saccharomyces cerevisiae.
Related PDB1g0v
[7]
CommentsX-ray crystallography
PubMed ID12127998
JournalBiochem Biophys Res Commun
Year2002
Volume295
Pages1020-6
AuthorsGustchina A, Li M, Phylip LH, Lees WE, Kay J, Wlodawer A
TitleAn unusual orientation for Tyr75 in the active site of the aspartic proteinase from Saccharomyces cerevisiae.
Related PDB1fmu,1fmx
[8]
PubMed ID15065849
JournalBiochemistry
Year2004
Volume43
Pages4071-81
AuthorsGreen TB, Ganesh O, Perry K, Smith L, Phylip LH, Logan TM, Hagen SJ, Dunn BM, Edison AS
TitleIA3, an aspartic proteinase inhibitor from Saccharomyces cerevisiae, is intrinsically unstructured in solution.

comments
This enzyme belongs to the peptidase family-A1. As it has a catalytic dyad composed of two aspartic acid residues, it must have a similar mechanism to that of pepsin (D00436 in EzCatDB).

createdupdated
2004-03-252012-06-27
Copyright: Nozomi Nagano, JST & CBRC-AIST
Funded by PRESTO/Japan Science and Technology Corporation (JST) (December 2001 - November 2004)
Funded by Grant-in-Aid for Publication of Scientific Research Results/Japan Society for the Promotion of Science (JSPS) (April 2005 - March 2006)
Funded by Grant-in-Aid for Scientific Research (B)/Japan Society for the Promotion of Science (JSPS) (April 2005 - March 2008)
Funded by BIRD/Japan Science and Technology Corporation (JST) (September 2005 - September 2008)
Funded by BIRD/Japan Science and Technology Corporation (JST) (October 2007 - September 2010)
Funded by Grant-in-Aid for Publication of Scientific Research Results/Japan Society for the Promotion of Science (JSPS) (April 2011 - March 2012)
Funded by Grant-in-Aid for Publication of Scientific Research Results/Japan Society for the Promotion of Science (JSPS) (April 2012 - March 2013)
Supported by the commission for the Development of Artificial Gene Synthesis Technology for Creating Innovative Biomaterial from the Ministry of Economy, Trade and Industry (METI) (October 2012 - )
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