KEGG   ENZYME: 3.4.21.50Help
Entry
EC 3.4.21.50                Enzyme                                 

Name
lysyl endopeptidase;
Achromobacter proteinase I (also see Comment);
Achromobacter lyticus alkaline proteinase I;
protease I;
achromopeptidase;
lysyl bond specific proteinase
Class
Hydrolases;
Acting on peptide bonds (peptidases);
Serine endopeptidases
BRITE hierarchy
Reaction(IUBMB)
Preferential cleavage: Lys!, including -Lys!Pro-
Comment
From Achromobacter lyticus [6]. Enzymes with similar specificity are produced by Lysobacter enzymogenes (Endoproteinase Lys-C; [3]) and Pseudomonas aeruginosa (Ps-1; [4]). In peptidase family S1 (trypsin family)
History
EC 3.4.21.50 created 1983
Orthology
K01337  lysyl endopeptidase
Genes
XCC: XCC2821
XCB: XC_1291
XCA: xcc-b100_1339
XCP: XCR_3194
XCV: XCV3140
XAX: XACM_2926
XAC: XAC2992
XCI: XCAW_03271
XCT: J151_03177
XCU: J159_03152
XOO: XOO1266
XOM: XOO1164(XOO1164)
XOP: PXO_02206
XAL: XALC_2516
XPH: XppCFBP6546_20795(XppCFBP6546P_20795)
LAB: LA76x_1946(prpL) LA76x_3979(lieA) LA76x_3980(lieA)
LAQ: GLA29479_1560(prpL) GLA29479_3571(lieA) GLA29479_3572(lieA)
LEM: LEN_1307(lyepB) LEN_1308(lyepA) LEN_1765 LEN_4452
PAE: PA4175(piv)
PAEV: N297_4307(prpL)
PAEI: N296_4307(prpL)
PAU: PA14_09900(prpL)
PAG: PLES_07521(piv)
PAF: PAM18_0762(piv)
PNC: NCGM2_5378(prpL)
PAEB: NCGM1900_0781(prpL)
PAEP: PA1S_03945
PAEM: U769_03975
PAEL: T223_03880
PAEU: BN889_04642(piv_1) BN889_04643(piv_2)
PAEG: AI22_29670
PAEC: M802_4305(prpL)
PAEO: M801_4173(prpL)
SWD: Swoo_0115
AAV: Aave_4238
AJS: Ajs_3699
AAA: Acav_4121
ACRA: BSY15_1975
VEI: Veis_4069
DAC: Daci_5718
CTES: O987_25540
HAU: Haur_0489
PSAC: PSM36_2730
DORI: FH5T_20685
MBAS: ALGA_4424
SRU: SRU_1622
SRM: SRM_01822(prpL)
FLN: FLA_2775
SGN: SGRA_2830
NDO: DDD_1941
WIN: WPG_3067
MOX: DAMO_3107
 » show all
Taxonomy
Reference
1  [PMID:6791693]
  Authors
Masaki T, Tanabe M, Nakamura K, Soejima M.
  Title
Studies on a new proteolytic enzyme from A chromobacter lyticus M497-1. I. Purification and some enzymatic properties.
  Journal
Biochim. Biophys. Acta. 660 (1981) 44-50.
Reference
2  [PMID:6168293]
  Authors
Masaki T, Fujihashi T, Nakamura K, Soejima M.
  Title
Studies on a new proteolytic enzyme from Achromobacter lyticus M497-1. II. specificity and inhibition studies of Achromobacter protease I.
  Journal
Biochim. Biophys. Acta. 660 (1981) 51-5.
Reference
3  [PMID:6359954]
  Authors
Jekel PA, Weijer WJ, Beintema JJ.
  Title
Use of endoproteinase Lys-C from Lysobacter enzymogenes in protein sequence analysis.
  Journal
Anal. Biochem. 134 (1983) 347-54.
Reference
4  [PMID:3090046]
  Authors
Elliott BW Jr, Cohen C.
  Title
Isolation and characterization of a lysine-specific protease from Pseudomonas aeruginosa.
  Journal
J. Biol. Chem. 261 (1986) 11259-65.
Reference
5  [PMID:2684982]
  Authors
Ohara T, Makino K, Shinagawa H, Nakata A, Norioka S, Sakiyama F.
  Title
Cloning, nucleotide sequence, and expression of Achromobacter protease I gene.
  Journal
J. Biol. Chem. 264 (1989) 20625-31.
  Sequence
Reference
6  [PMID:2492988]
  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.
  Journal
J. Biol. Chem. 264 (1989) 3832-9.
  Sequence
Other DBs
ExplorEnz - The Enzyme Database: 3.4.21.50
IUBMB Enzyme Nomenclature: 3.4.21.50
ExPASy - ENZYME nomenclature database: 3.4.21.50
BRENDA, the Enzyme Database: 3.4.21.50
CAS: 123175-82-6

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