DB code: D00430

RLCP classification 1.13.30000.10 : Hydrolysis
CATH domain 2.40.10.10 : Thrombin, subunit H Catalytic domain
2.40.10.10 : Thrombin, subunit H Catalytic domain
E.C. 3.4.21.50
CSA
M-CSA
MACiE

CATH domain Related DB codes (homologues)
2.40.10.10 : Thrombin, subunit H M00139 D00214 M00167 D00426 M00133 D00428 D00429 D00431 D00432 D00433 D00434 D00435 M00227 M00209 D00194 D00197 D00211 D00212 D00216 M00212 D00224 D00497 M00217 M00216 D00528 D00848 D00850 D00851 D00852 D00855 M00152 M00155 M00157 M00181 M00315 M00316 M00317 M00348 M00349 T00074 T00410 T00411

Uniprot Enzyme Name
UniprotKB Protein name Synonyms MEROPS Pfam
P15636 Protease 1
EC 3.4.21.50
Protease I
API
Lysyl endopeptidase
S01.280 (Serine)
PF01483 (P_proprotein)
PF00801 (PKD)
[Graphical View]

KEGG enzyme name
lysyl endopeptidase
Achromobacter proteinase I (also see Comment)
Achromobacter lyticus alkaline proteinase I
protease I
achromopeptidase
lysyl bond specific proteinase

UniprotKB: Accession Number Entry name Activity Subunit Subcellular location Cofactor
P15636 API_ACHLY Preferential cleavage: Lys-|-Xaa, including Lys-|-Pro. Secreted.

KEGG Pathways
Map code Pathways E.C.

Compound table
Substrates Products Intermediates
KEGG-id C00017 C00012 C00001 C00017 C00012 I00087 I00085 I00086
E.C.
Compound Protein Peptide H2O Protein Peptide Peptidyl-tetrahedral intermediate Acyl-enzyme Tetrahedral intermediate
Type peptide/protein peptide/protein H2O peptide/protein peptide/protein
ChEBI 15377
PubChem 22247451
962
1arbA01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound
1arcA01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Analogue:TCK Unbound Unbound
1arbA02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound
1arcA02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound

Reference for Active-site residues
resource references E.C.
Swiss-prot;P15636 & literature[2]

Active-site residues
PDB Catalytic residues Cofactor-binding residues Modified residues Main-chain involved in catalysis Comment
1arbA01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain SER 194 GLY 192;SER 194
1arcA01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain SER 194 GLY 192;SER 194
1arbA02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain HIS 57;ASP 113
1arcA02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain HIS 57;ASP 113

References for Catalytic Mechanism
References Sections No. of steps in catalysis
[3]
Fig.6, p.4157

References
[1]
Resource
Comments X-ray crystallography
Medline ID
PubMed ID 2492988
Journal J Biol Chem
Year 1989
Volume 264
Pages 3832-9
Authors Tsunasawa S, Masaki T, Hirose M, Soejima M, Sakiyama F
Title The primary structure and structural characteristics of Achromobacter lyticus protease I, a lysine-specific serine protease.
Related PDB 1arb 1arc
Related UniProtKB
[2]
Resource
Comments
Medline ID
PubMed ID 7845202
Journal Methods Enzymol
Year 1994
Volume 244
Pages 126-37
Authors Sakiyama F, Masaki T
Title Lysyl endopeptidase of Achromobacter lyticus.
Related PDB
Related UniProtKB
[3]
Resource
Comments
Medline ID
PubMed ID 12180992
Journal Eur J Biochem
Year 2002
Volume 269
Pages 4152-8
Authors Shiraki K, Norioka S, Li S, Yokota K, Sakiyama F
Title Electrostatic role of aromatic ring stacking in the pH-sensitive modulation of a chymotrypsin-type serine protease, Achromobacter protease I.
Related PDB
Related UniProtKB
[4]
Resource
Comments
Medline ID
PubMed ID 11820934
Journal J Biochem (Tokyo)
Year 2002
Volume 131
Pages 213-8
Authors Shiraki K, Norioka S, Li S, Sakiyama F
Title Contribution of an imidazole-indole stack to high catalytic potency of a lysine-specific serine protease, Achromobacter protease I.
Related PDB
Related UniProtKB

Comments
According to the papers [2], [3] & [4], this enzyme has got a similar catalytic triad to that of trypsin, suggesting a similar catalytic mechanism.
This enzyme belongs to the peptidase family-S5.

Created Updated
2004-04-27 2011-02-18