KEGG   ENZYME: 3.4.24.25Help
Entry
EC 3.4.24.25                Enzyme                                 

Name
vibriolysin;
Aeromonas proteolytica neutral proteinase;
aeromonolysin
Class
Hydrolases;
Acting on peptide bonds (peptidases);
Metalloendopeptidases
BRITE hierarchy
Reaction(IUBMB)
Preferential cleavage of bonds with bulky hydrophobic groups in P2 and P1'. Phe at P1' is the most favoured residue, which distinguished this enzyme from thermolysin
Comment
Thermostable enzyme from Vibrio proteolyticus (formerly Aeromonas proteolytica). Specificity related to, but distinct from, those of thermolysin and bacillolysin [1]. A zinc metallopeptidase in family M4 (thermolysin family). Formerly included in EC 3.4.24.4
History
EC 3.4.24.25 created 1972 as EC 3.4.24.4, part transferred 1992 to EC 3.4.24.25, modified 1997
Orthology
K08604  vibriolysin
Genes
XSA: SB85_15700
LAB: LA76x_2473(nprV) LA76x_2475
LAQ: GLA29479_1171(empA) GLA29479_1174(hap)
LCP: LC55x_2887(nprV) LC55x_2889 LC55x_2891
LGU: LG3211_2739 LG3211_2741(nprV) LG3211_4445
LEZ: GLE_2741(nprV) GLE_2743(nprV)
LEM: LEN_2283 LEN_2284
LMB: C9I47_0200
LYT: DWG18_10025
DTX: ATSB10_19710
VCH: VCA0865
VCS: MS6_A0903
VCE: Vch1786_II0554(hap)
VCI: O3Y_17553
VCO: VC0395_0371(hap)
VCR: VC395_A0889(hap)
VCM: VCM66_A0824(hap)
VCX: VAA049_2123(hap)
VCZ: VAB027_324(hap)
VVU: VV2_0974
VVY: VVA1465
VVL: VV93_v1c43660(lasB)
VPA: VPA0755
VSP: VS_1267(vsm)
VAN: VAA_01306
VAU: VANGNB10_cII0919c(empA)
SDN: Sden_3015
SBL: Sbal_3874
PSM: PSM_B0576
PSEN: PNC201_18505(empA)
MVS: MVIS_1898(empA) MVIS_2920(empA)
MYA: MORIYA_1508(nprV) MORIYA_2361(nprV)
SAGA: M5M_18570
LPN: lpg0019
LPH: LPV_0023
LPO: LPO_0020
LPM: LP6_0020
LPF: lpl0020
LPP: lpp0019
LPC: LPC_0020
LPA: lpa_00026
LPE: lp12_0019
LLO: LLO_0045
LFA: LFA_0023
PSAL: PSLF89_34
TIG: THII_0643
HCH: HCH_02479
KKO: Kkor_0311
KGE: TQ33_2045
AHA: AHA_0851
AVR: B565_3414
AMED: B224_0573
ASR: WL1483_2962(nprV)
ACAV: VI35_03960
MXA: MXAN_6106(fibA)
CCX: COCOR_00680(fibA1) COCOR_05260(empA) COCOR_05722(nprV) COCOR_06634(fibA)
 » show all
Taxonomy
Reference
1  [PMID:2276]
  Authors
Holmquist B, Vallee BL.
  Title
Esterase activity of zinc neutral proteases.
  Journal
Biochemistry 15:101-7 (1976)
Reference
2  [PMID:1012006]
  Authors
Wilkes SH, Prescott JM.
  Title
Aeromonas neutral protease.
  Journal
Methods Enzymol 45:404-15 (1976)
DOI:10.1016/S0076-6879(76)45036-X
Reference
3  [PMID:7000005]
  Authors
Bayliss ME, Wilkes SH, Prescott JM.
  Title
Aeromonas neutral protease: specificity toward extended substrates.
  Journal
Arch Biochem Biophys 204:214-9 (1980)
DOI:10.1016/0003-9861(80)90026-0
Reference
4  [PMID:3123480]
  Authors
Wilkes SH, Bayliss ME, Prescott JM.
  Title
Critical ionizing groups in Aeromonas neutral protease.
  Journal
J Biol Chem 263:1821-5 (1988)
Reference
5  [PMID:1551587]
  Authors
David VA, Deutch AH, Sloma A, Pawlyk D, Ally A, Durham DR
  Title
Cloning, sequencing and expression of the gene encoding the extracellular neutral protease, vibriolysin, of Vibrio proteolyticus.
  Journal
Gene 112:107-12 (1992)
DOI:10.1016/0378-1119(92)90310-L
  Sequence
Other DBs
ExplorEnz - The Enzyme Database: 3.4.24.25
IUBMB Enzyme Nomenclature: 3.4.24.25
ExPASy - ENZYME nomenclature database: 3.4.24.25
BRENDA, the Enzyme Database: 3.4.24.25
CAS: 69598-88-5

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