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 15377 |
||||||||||
| PubChem |
22247451 962 22247451 962 |
||||||||||
| 1qdmA01 |
|
|
|
|
|
Unbound | Unbound | Unbound | Unbound | Unbound | |
| 1qdmB01 |
|
|
|
|
|
Unbound | Unbound | Unbound | Unbound | Unbound | |
| 1qdmC01 |
|
|
|
|
|
Unbound | Unbound | Unbound | Unbound | Unbound | |
| 1qdmA02 |
|
|
|
|
|
Unbound | Unbound | Unbound | Unbound | Unbound | |
| 1qdmB02 |
|
|
|
|
|
Unbound | Unbound | Unbound | Unbound | Unbound | |
| 1qdmC02 |
|
|
|
|
|
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 |
|
|
|
|
|
ASP 36 | ||||
| 1qdmB01 |
|
|
|
|
|
ASP 36 | ||||
| 1qdmC01 |
|
|
|
|
|
ASP 36 | ||||
| 1qdmA02 |
|
|
|
|
|
ASP 223 | ||||
| 1qdmB02 |
|
|
|
|
|
ASP 223 | ||||
| 1qdmC02 |
|
|
|
|
|
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, |
| Created | Updated |
|---|---|
| 2004-10-29 | 2012-06-28 |