EzCatDB: D00445
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DB codeD00445
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.3.4.23.40

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,D00484,M00206,M00166,D00231,D00529

Enzyme Name
UniProtKBKEGG

P42210
Protein namePhytepsinphytepsin
SynonymsEC 3.4.23.40
Aspartic proteinase
ContainsPhytepsin 32 kDa subunit
Phytepsin 29 kDa subunit
Phytepsin 16 kDa subunit
Phytepsin 11 kDa subunit
MEROPSA01.020 (Aspartic)
PfamPF00026 (Asp)
PF05184 (SapB_1)
PF03489 (SapB_2)
[Graphical view]


UniProtKB:Accession NumberP42210
Entry nameASPR_HORVU
ActivityPrefers hydrophobic residues Phe, Val, Ile, Leu, and Ala at P1 and P1'', but also cleaves -Phe-|-Asp- and -Asp-|-Asp- bonds in 2S albumin from plant seeds.
SubunitHeterodimer of two subunits (29 kDa and 11 kDa) processed from the precursor molecule. A large enzyme (32 kDa and 16 kDa) is an intermediate precursor form.
Subcellular locationVacuole.
Cofactor

Compound table: links to PDB-related databases & PoSSuM

SubstratesProductsintermediates
KEGG-idC00012C00017C00001C00012C00017I00136
CompoundPeptideProteinH2OPeptideProteinAmino-diol-tetrahedral intermediate
Typepeptide/proteinpeptide/proteinH2Opeptide/proteinpeptide/protein
ChEBI

15377



PubChem

962
22247451



              
1qdmA01UnboundUnbound UnboundUnboundUnbound
1qdmB01UnboundUnbound UnboundUnboundUnbound
1qdmC01UnboundUnbound UnboundUnboundUnbound
1qdmA02UnboundUnbound UnboundUnboundUnbound
1qdmB02UnboundUnbound UnboundUnboundUnbound
1qdmC02UnboundUnbound UnboundUnboundUnbound

Active-site residues
resource
Swiss-prot;P42210
pdbCatalytic residues
         
1qdmA01ASP 36
1qdmB01ASP 36
1qdmC01ASP 36
1qdmA02ASP 223
1qdmB02ASP 223
1qdmC02ASP 223


references
[1]
PubMed ID1812727
JournalAdv Exp Med Biol
Year1991
Volume306
Pages355-9
AuthorsTormakangas K, Runeberg-Roos P, Ostman A, Tilgmann C, Sarkkinen P, Kervinen J, Mikola L, Kalkkinen N
TitleAspartic proteinase from barley seeds is related to animal cathepsin D.
[2]
PubMed ID7925961
JournalFEBS Lett
Year1994
Volume352
Pages131-6
AuthorsGuruprasad K, Tormakangas K, Kervinen J, Blundell TL
TitleComparative modelling of barley-grain aspartic proteinase: a structural rationale for observed hydrolytic specificity.
[3]
PubMed ID10607668
JournalCurr Opin Struct Biol
Year1999
Volume9
Pages684-9
AuthorsBernstein NK, James MN
TitleNovel ways to prevent proteolysis - prophytepsin and proplasmepsin II.
[4]
CommentsX-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS)
Medline ID99335466
PubMed ID10406799
JournalEMBO J
Year1999
Volume18
Pages3947-55
AuthorsKervinen J, Tobin GJ, Costa J, Waugh DS, Wlodawer A, Zdanov A
TitleCrystal structure of plant aspartic proteinase prophytepsin: inactivation and vacuolar targeting.
Related PDB1qdm
Related UniProtKBP42210
[5]
PubMed ID11330695
JournalBiosci Biotechnol Biochem
Year2001
Volume65
Pages702-5
AuthorsPark H, Kusakabe I, Sakakibara Y, Kobayashi H
TitleAutoproteolytic processing of aspartic proteinase from sunflower seeds.
[6]
PubMed ID15153096
JournalEur J Biochem
Year2004
Volume271
Pages2067-75
AuthorsSimoes I, Faro C
TitleStructure and function of plant aspartic proteinases.

comments
This enzyme belongs to the peptidase family-A1.
This enzyme has got a catalytic dyad, composed of two aspartic acid residues, which is the same as that of other aspartate proteases such as pepsin (D00436 in EzCatDB). It suggests that it may have a similar reaction mechanism to that of these enzymes.

createdupdated
2004-10-292012-06-28


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Funded by Grant-in-Aid for Publication of Scientific Research Results/Japan Society for the Promotion of Science (JSPS) (April 2005 - March 2006)
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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)
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