DB code: D00231
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. | 3.4.23.25 | |
CSA | 2jxr | |
M-CSA | 2jxr | |
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 D00445 D00484 M00206 M00166 D00529 |
Uniprot Enzyme Name | UniprotKB | Protein name | Synonyms | RefSeq | MEROPS | Pfam |
---|---|---|---|---|---|
P07267 |
Saccharopepsin
|
EC
3.4.23.25
Aspartate protease Proteinase A Proteinase YSCA Carboxypeptidase Y-deficient protein 4 |
NP_015171.1
(Protein)
NM_001183968.1 (DNA/RNA sequence) |
A01.018
(Aspartic)
|
PF00026
(Asp)
[Graphical View] |
KEGG enzyme name |
---|
saccharopepsin
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 |
UniprotKB: Accession Number | Entry name | Activity | Subunit | Subcellular location | Cofactor |
---|---|---|---|---|---|
P07267 | CARP_YEAST | Hydrolysis 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. | Vacuole. Note=Lysosome-like vacuoles. |
KEGG Pathways | Map code | Pathways | E.C. |
---|
Compound table | |||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|
Substrates | Products | Intermediates | |||||||||
KEGG-id | C00017 | C00012 | C00001 | C00017 | C00012 | I00136 | |||||
E.C. | |||||||||||
Compound | Protein | Peptide | H2O | Protein | Peptide | Amino-diol-tetrahedral intermediate | |||||
Type | peptide/protein | peptide/protein | H2O | peptide/protein | peptide/protein | ||||||
ChEBI |
15377 15377 |
||||||||||
PubChem |
22247451 962 22247451 962 |
||||||||||
1dp5A01 | Unbound | Unbound | Unbound | Unbound | Unbound | ||||||
1dpjA01 | Unbound | Unbound | Unbound | Unbound | Unbound | ||||||
1fmuA01 | Unbound | Unbound | Unbound | Unbound | Unbound | ||||||
1fmxA01 | Unbound | Unbound | Unbound | Unbound | Unbound | ||||||
1fmxB01 | Unbound | Unbound | Unbound | Unbound | Unbound | ||||||
1fq4A01 | Unbound | Analogue:2Y2 | Unbound | Unbound | Unbound | ||||||
1fq5A01 | Unbound | Analogue:0GM | Unbound | Unbound | Unbound | ||||||
1fq6A01 | Unbound | Analogue:0QF | Unbound | Unbound | Unbound | ||||||
1fq7A01 | Unbound | Analogue:2Y3 | Unbound | Unbound | Unbound | ||||||
1fq8A01 | Unbound | Analogue:2Y4 | Unbound | Unbound | Unbound | ||||||
1g0vA01 | Unbound | Unbound | Unbound | Unbound | Unbound | ||||||
1jxrA01 | Unbound | Unbound | Unbound | Unbound | Transition-state-analogue:MOR-PHE-NLE-CHF-NME (chain I) | ||||||
2jxrA01 | Unbound | Unbound | Unbound | Unbound | Transition-state-analogue:2Z3 | ||||||
1dp5A02 | Unbound | Unbound | Unbound | Unbound | Unbound | ||||||
1dpjA02 | Unbound | Unbound | Unbound | Unbound | Unbound | ||||||
1fmuA02 | Unbound | Unbound | Unbound | Unbound | Unbound | ||||||
1fmxA02 | Unbound | Unbound | Unbound | Unbound | Unbound | ||||||
1fmxB02 | Unbound | Unbound | Unbound | Unbound | Unbound | ||||||
1fq4A02 | Unbound | Unbound | Unbound | Unbound | Unbound | ||||||
1fq5A02 | Unbound | Unbound | Unbound | Unbound | Unbound | ||||||
1fq6A02 | Unbound | Unbound | Unbound | Unbound | Unbound | ||||||
1fq7A02 | Unbound | Unbound | Unbound | Unbound | Unbound | ||||||
1fq8A02 | Unbound | Unbound | Unbound | Unbound | Unbound | ||||||
1g0vA02 | Unbound | Unbound | Unbound | Unbound | Unbound | ||||||
1jxrA02 | Unbound | Unbound | Unbound | Unbound | Unbound | ||||||
2jxrA02 | Unbound | Unbound | Unbound | Unbound | Unbound |
Reference for Active-site residues | ||
---|---|---|
resource | references | E.C. |
Swiss-prot;P07267 |
Active-site residues | ||||||||||
---|---|---|---|---|---|---|---|---|---|---|
PDB | Catalytic residues | Cofactor-binding residues | Modified residues | Main-chain involved in catalysis | Comment | |||||
1dp5A01 | ASP 32 | |||||||||
1dpjA01 | ASP 32 | |||||||||
1fmuA01 | ASP 32 | |||||||||
1fmxA01 | ASP 33 | |||||||||
1fmxB01 | ASP 33 | |||||||||
1fq4A01 | ASP 32 | |||||||||
1fq5A01 | ASP 32 | |||||||||
1fq6A01 | ASP 32 | |||||||||
1fq7A01 | ASP 32 | |||||||||
1fq8A01 | ASP 32 | |||||||||
1g0vA01 | ASP 32 | |||||||||
1jxrA01 | ASP 32 | |||||||||
2jxrA01 | ASP 32 | |||||||||
1dp5A02 | ASP 215 | |||||||||
1dpjA02 | ASP 215 | |||||||||
1fmuA02 | ASP 217 | |||||||||
1fmxA02 | ASP 218 | |||||||||
1fmxB02 | ASP 218 | |||||||||
1fq4A02 | ASP 215 | |||||||||
1fq5A02 | ASP 215 | |||||||||
1fq6A02 | ASP 215 | |||||||||
1fq7A02 | ASP 215 | |||||||||
1fq8A02 | ASP 215 | |||||||||
1g0vA02 | ASP 215 | |||||||||
1jxrA02 | ASP 215 | mutant L315I | ||||||||
2jxrA02 | ASP 215 | mutant L315I |
References for Catalytic Mechanism | ||
---|---|---|
References | Sections | No. of steps in catalysis |
[3]
|
References | |
---|---|
[1] | |
Resource | |
Comments | |
Medline ID | |
PubMed ID | 1959673 |
Journal | FEBS Lett |
Year | 1991 |
Volume | 293 |
Pages | 62-6 |
Authors | Rupp S, Hirsch HH, Wolf DH |
Title |
Biogenesis of the yeast vacuole (lysosome). |
Related PDB | |
Related UniProtKB | |
[2] | |
Resource | |
Comments | |
Medline ID | |
PubMed ID | 8540315 |
Journal | Adv Exp Med Biol |
Year | 1995 |
Volume | 362 |
Pages | 155-66 |
Authors | Aguilar CF, Dhanaraj V, Guruprasad K, Dealwis C, Badasso M, Cooper JB, Wood SP, Blundell TL |
Title |
Comparisons of the three-dimensional structures, |
Related PDB | |
Related UniProtKB | |
[3] | |
Resource | |
Comments | X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) |
Medline ID | 97280793 |
PubMed ID | 9135120 |
Journal | J Mol Biol |
Year | 1997 |
Volume | 267 |
Pages | 899-915 |
Authors | Aguilar CF, Cronin NB, Badasso M, Dreyer T, Newman MP, Cooper JB, Hoover DJ, Wood SP, Johnson MS, Blundell TL |
Title | The three-dimensional structure at 2.4 A resolution of glycosylated proteinase A from the lysosome-like vacuole of Saccharomyces cerevisiae. |
Related PDB | 1jxr 2jxr |
Related UniProtKB | P07267 |
[4] | |
Resource | |
Comments | X-ray crystallography |
Medline ID | |
PubMed ID | 11061973 |
Journal | J Mol Biol |
Year | 2000 |
Volume | 303 |
Pages | 745-60 |
Authors | Cronin NB, Badasso MO, J Tickle I, Dreyer T, Hoover DJ, Rosati RL, Humblet CC, Lunney EA, Cooper JB |
Title | X-ray structures of five renin inhibitors bound to saccharopepsin: exploration of active-site specificity. |
Related PDB | 1fq4 1fq5 1fq6 1fq7 1fq8 |
Related UniProtKB | |
[5] | |
Resource | |
Comments | X-ray crystallography |
Medline ID | |
PubMed ID | 10655612 |
Journal | Nat Struct Biol |
Year | 2000 |
Volume | 7 |
Pages | 113-7 |
Authors | Li M, Phylip LH, Lees WE, Winther JR, Dunn BM, Wlodawer A, Kay J, Gustchina A |
Title | The aspartic proteinase from Saccharomyces cerevisiae folds its own inhibitor into a helix. |
Related PDB | 1dp5 1dpj |
Related UniProtKB | |
[6] | |
Resource | |
Comments | X-ray crystallography |
Medline ID | |
PubMed ID | 11042188 |
Journal | J Biol Chem |
Year | 2001 |
Volume | 276 |
Pages | 2023-30 |
Authors | Phylip LH, Lees WE, Brownsey BG, Bur D, Dunn BM, Winther JR, Gustchina A, Li M, Copeland T, Wlodawer A, Kay J |
Title | The potency and specificity of the interaction between the IA3 inhibitor and its target aspartic proteinase from Saccharomyces cerevisiae. |
Related PDB | 1g0v |
Related UniProtKB | |
[7] | |
Resource | |
Comments | X-ray crystallography |
Medline ID | |
PubMed ID | 12127998 |
Journal | Biochem Biophys Res Commun |
Year | 2002 |
Volume | 295 |
Pages | 1020-6 |
Authors | Gustchina A, Li M, Phylip LH, Lees WE, Kay J, Wlodawer A |
Title | An unusual orientation for Tyr75 in the active site of the aspartic proteinase from Saccharomyces cerevisiae. |
Related PDB | 1fmu 1fmx |
Related UniProtKB | |
[8] | |
Resource | |
Comments | |
Medline ID | |
PubMed ID | 15065849 |
Journal | Biochemistry |
Year | 2004 |
Volume | 43 |
Pages | 4071-81 |
Authors | Green TB, Ganesh O, Perry K, Smith L, Phylip LH, Logan TM, Hagen SJ, Dunn BM, Edison AS |
Title |
IA3, |
Related PDB | |
Related UniProtKB |
Comments |
---|
This enzyme belongs to the peptidase family-A1. |
Created | Updated |
---|---|
2004-03-25 | 2012-06-27 |