KEGG   ENZYME: 3.4.24.20Help
Entry
EC 3.4.24.20                Enzyme                                 

Name
peptidyl-Lys metalloendopeptidase;
Armillaria mellea neutral proteinase;
peptidyllysine metalloproteinase
Class
Hydrolases;
Acting on peptide bonds (peptidases);
Metalloendopeptidases
BRITE hierarchy
Reaction(IUBMB)
Preferential cleavage in proteins: -Xaa!Lys- (in which Xaa may be Pro)
Comment
From the honey fungus Armillaria mellea. In peptidase family M35 (deuterolysin family).
History
EC 3.4.24.20 created 1978 as EC 3.4.99.32, transferred 1992 to EC 3.4.24.20 (EC 3.4.99.30 created 1978, incorporated 1992)
Orthology
K08646  peptidyl-Lys metalloendopeptidase
Genes
AQU: 105313500 105314928 105316327 105316701 109583088 109583394
CFJ: CFIO01_05061
ELA: UCREL1_2147
PFY: PFICI_00158
TVS: TRAVEDRAFT_130231 TRAVEDRAFT_158002
DSQ: DICSQDRAFT_109441 DICSQDRAFT_131350 DICSQDRAFT_156505
HIR: HETIRDRAFT_56025
PSQ: PUNSTDRAFT_106817 PUNSTDRAFT_127742
ADL: AURDEDRAFT_116343 AURDEDRAFT_129434 AURDEDRAFT_129499 AURDEDRAFT_173431 AURDEDRAFT_44005 AURDEDRAFT_73170 AURDEDRAFT_73958
GTR: GLOTRDRAFT_67866
ABP: AGABI1DRAFT110574(AGABI1DRAFT_110574) AGABI1DRAFT115620(AGABI1DRAFT_115620)
ABV: AGABI2DRAFT189525(AGABI2DRAFT_189525) AGABI2DRAFT194132(AGABI2DRAFT_194132)
XCP: XCR_2945
XCV: XCV2918
XAX: XACM_2704
XAC: XAC2763
XOO: XOO3300
XOM: XOO3123(XOO3123)
XOP: PXO_01896
XOR: XOC_1688
XPH: XppCFBP6546_22060(XppCFBP6546P_22060)
LAB: LA76x_2180(mep) LA76x_2225(mep)
LCP: LC55x_2157(mep) LC55x_2457(mep)
LGU: LG3211_0892(mep) LG3211_3069(mep)
LEZ: GLE_3062(eprA1)
LEM: LEN_1975
PFL: PFL_4985
PPRO: PPC_4986
SAZ: Sama_1205
SLO: Shew_1243
SWD: Swoo_1511
AHA: AHA_2713
AMED: B224_2992
ASR: WL1483_3350(eprA1)
ACAV: VI35_13060
CVI: CV_3506
CFU: CFU_3438
CARE: LT85_3938
CPRA: CPter91_4254(mep)
CCX: COCOR_02766(eprA1) COCOR_03205(eprA2)
ASE: ACPL_4120
ACTS: ACWT_3991
 » show all
Taxonomy
Reference
1  [PMID:1239277]
  Authors
Doonan S, Doonan HJ, Hanford R, Vernon CA, Walker JM, da Airold LP, Bossa F, Barra D, Carloni M, Fasella P, Riva F.
  Title
The primary structure of aspartate aminotransferase from pig heart muscle. Digestion with a proteinase having specificity for lysine residues.
  Journal
Biochem J 149:497-506 (1975)
Reference
2  [PMID:23849]
  Authors
Lewis WG, Basford JM, Walton PL.
  Title
Specificity and inhibition studies of Armillaria mellea protease.
  Journal
Biochim Biophys Acta 522:551-60 (1978)
DOI:10.1016/0005-2744(78)90087-6
  Sequence
Other DBs
ExplorEnz - The Enzyme Database: 3.4.24.20
IUBMB Enzyme Nomenclature: 3.4.24.20
ExPASy - ENZYME nomenclature database: 3.4.24.20
BRENDA, the Enzyme Database: 3.4.24.20
CAS: 65979-41-1

DBGET integrated database retrieval system