DB code: D00445

RLCP classification 1.13.200.966 : Hydrolysis
CATH domain 2.40.70.10 : Cathepsin D, subunit A; domain 1 Catalytic domain
2.40.70.10 : Cathepsin D, subunit A; domain 1 Catalytic domain
E.C. 3.4.23.40
CSA
M-CSA
MACiE

CATH domain Related DB codes (homologues)
2.40.70.10 : Cathepsin D, subunit A; domain 1 D00471 D00436 D00438 D00439 D00440 D00441 D00442 D00443 D00437 D00444 D00423 D00484 M00206 M00166 D00231 D00529

Uniprot Enzyme Name
UniprotKB Protein name Synonyms Contains MEROPS Pfam
P42210 Phytepsin
EC 3.4.23.40
Aspartic proteinase
Phytepsin 32 kDa subunit
Phytepsin 29 kDa subunit
Phytepsin 16 kDa subunit
Phytepsin 11 kDa subunit
A01.020 (Aspartic)
PF00026 (Asp)
PF05184 (SapB_1)
PF03489 (SapB_2)
[Graphical View]

KEGG enzyme name
phytepsin

UniprotKB: Accession Number Entry name Activity Subunit Subcellular location Cofactor
P42210 ASPR_HORVU Prefers 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. Heterodimer 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. Vacuole.

KEGG Pathways
Map code Pathways E.C.

Compound table
Substrates Products Intermediates
KEGG-id C00012 C00017 C00001 C00012 C00017 I00136
E.C.
Compound Peptide Protein H2O Peptide Protein Amino-diol-tetrahedral intermediate
Type peptide/protein peptide/protein H2O peptide/protein peptide/protein
ChEBI 15377
PubChem 22247451
962
1qdmA01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound
1qdmB01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound
1qdmC01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound
1qdmA02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound
1qdmB02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound
1qdmC02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound

Reference for Active-site residues
resource references E.C.
Swiss-prot;P42210

Active-site residues
PDB Catalytic residues Cofactor-binding residues Modified residues Main-chain involved in catalysis Comment
1qdmA01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain ASP 36
1qdmB01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain ASP 36
1qdmC01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain ASP 36
1qdmA02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain ASP 223
1qdmB02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain ASP 223
1qdmC02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain ASP 223

References for Catalytic Mechanism
References Sections No. of steps in catalysis

References
[1]
Resource
Comments
Medline ID
PubMed ID 1812727
Journal Adv Exp Med Biol
Year 1991
Volume 306
Pages 355-9
Authors Tormakangas K, Runeberg-Roos P, Ostman A, Tilgmann C, Sarkkinen P, Kervinen J, Mikola L, Kalkkinen N
Title Aspartic proteinase from barley seeds is related to animal cathepsin D.
Related PDB
Related UniProtKB
[2]
Resource
Comments
Medline ID
PubMed ID 7925961
Journal FEBS Lett
Year 1994
Volume 352
Pages 131-6
Authors Guruprasad K, Tormakangas K, Kervinen J, Blundell TL
Title Comparative modelling of barley-grain aspartic proteinase: a structural rationale for observed hydrolytic specificity.
Related PDB
Related UniProtKB
[3]
Resource
Comments
Medline ID
PubMed ID 10607668
Journal Curr Opin Struct Biol
Year 1999
Volume 9
Pages 684-9
Authors Bernstein NK, James MN
Title Novel ways to prevent proteolysis - prophytepsin and proplasmepsin II.
Related PDB
Related UniProtKB
[4]
Resource
Comments X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS)
Medline ID 99335466
PubMed ID 10406799
Journal EMBO J
Year 1999
Volume 18
Pages 3947-55
Authors Kervinen J, Tobin GJ, Costa J, Waugh DS, Wlodawer A, Zdanov A
Title Crystal structure of plant aspartic proteinase prophytepsin: inactivation and vacuolar targeting.
Related PDB 1qdm
Related UniProtKB P42210
[5]
Resource
Comments
Medline ID
PubMed ID 11330695
Journal Biosci Biotechnol Biochem
Year 2001
Volume 65
Pages 702-5
Authors Park H, Kusakabe I, Sakakibara Y, Kobayashi H
Title Autoproteolytic processing of aspartic proteinase from sunflower seeds.
Related PDB
Related UniProtKB
[6]
Resource
Comments
Medline ID
PubMed ID 15153096
Journal Eur J Biochem
Year 2004
Volume 271
Pages 2067-75
Authors Simoes I, Faro C
Title Structure and function of plant aspartic proteinases.
Related PDB
Related UniProtKB

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.

Created Updated
2004-10-29 2012-06-28