DB code: D00430

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 15377
PubChem			22247451 962 22247451 962

1arbA01	Unbound	Unbound		Unbound	Unbound
1arcA01	Unbound	Analogue:TCK		Unbound	Unbound
1arbA02	Unbound	Unbound		Unbound	Unbound
1arcA02	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	SER 194			GLY 192;SER 194
1arcA01	SER 194			GLY 192;SER 194
1arbA02	HIS 57;ASP 113
1arcA02	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