KEGG   ENZYME: 3.4.21.62
Entry
EC 3.4.21.62                Enzyme                                 

Name
subtilisin;
alcalase;
alcalase 0.6L;
alcalase 2.5L;
ALK-enzyme;
bacillopeptidase A;
bacillopeptidase B;
Bacillus subtilis alkaline proteinase bioprase;
bioprase AL 15;
bioprase APL 30;
colistinase;
(see also comments);
subtilisin J;
subtilisin S41;
subtilisin Sendai;
subtilisin GX;
subtilisin E;
subtilisin BL;
genenase I;
esperase;
maxatase;
alcalase;
thermoase PC 10;
protease XXVII;
thermoase;
superase;
subtilisin DY;
subtilopeptidase;
SP 266;
savinase 8.0L;
savinase 4.0T;
kazusase;
protease VIII;
opticlean;
Bacillus subtilis alkaline proteinase;
protin A 3L;
savinase;
savinase 16.0L;
savinase 32.0 L EX;
orientase 10B;
protease S
Class
Hydrolases;
Acting on peptide bonds (peptidases);
Serine endopeptidases
Reaction(IUBMB)
Hydrolysis of proteins with broad specificity for peptide bonds, and a preference for a large uncharged residue in P1. Hydrolyses peptide amides
Comment
Subtilisin is a serine endopeptidase, type example of peptidase family S8. It contains no cysteine residues (although these are found in homologous enzymes). Species variants include subtilisin BPN' (also subtilisin B, subtilopeptidase B, subtilopeptidase C, Nagarse, Nagarse proteinase, subtilisin Novo, bacterial proteinase Novo) and subtilisin Carlsberg (subtilisin A, subtilopeptidase A, alcalase Novo). Similar enzymes are produced by various Bacillus subtilis strains and other Bacillus species [1,3]
History
EC 3.4.21.62 created 1992 (EC 3.4.21.14 created 1961 as EC 3.4.4.16, transferred 1972 to EC 3.4.21.14, modified 1986, part incorporated 1992)
Orthology
K01342  subtilisin
Genes
VNA: PN96_21170
VEJ: VEJY3_20426
PAZO: AYR47_08420
PPUU: PputUW4_00217
PFZ: AV641_21465
PPSY: AOC04_18875
PAGR: E2H98_07725
SPSW: Sps_01013
PSPO: PSPO_b1036
MII: BTJ40_12175
MICT: FIU95_10505(isp)
METL: U737_14160
GAI: IMCC3135_18295(aprE)
TOL: TOL_3513
AHA: AHA_3478
BAV: BAV2607
PNA: Pnap_1683
HPSE: HPF_14095
GBM: Gbem_3055
AOL: S58_68990
MSC: BN69_1924
DSH: Dshi_0257
MALG: MALG_02172
ERF: FIU90_00740(apr1)
SHUM: STHU_11850
BSU: BSU10300(aprE)
BSR: I33_1162
BSL: A7A1_3704
BSH: BSU6051_10300(aprE)
BSUT: BSUB_01127(aprE)
BSUL: BSUA_01127(aprE)
BSUS: Q433_05825
BSS: BSUW23_05210(aprE)
BST: GYO_1328
BSO: BSNT_07467(aprN)
BSQ: B657_10300(aprE)
BSX: C663_1054(aprE) C663_3243(aprX)
BLI: BL01111(apr)
BLD: BLi01109(apr)
BLH: BaLi_c12310(aprE)
BAQ: BACAU_1010(aprE)
BYA: BANAU_0954(aprE)
BAMP: B938_05060
BAML: BAM5036_0953(aprE)
BAMA: RBAU_1012(aprE)
BAMN: BASU_0989(aprE)
BAMB: BAPNAU_2748(aprE)
BAMT: AJ82_05900
BAMY: V529_09920
BMP: NG74_01058(apr)
BAO: BAMF_1119(aprE)
BAZ: BAMTA208_04835(aprE)
BQL: LL3_01118(aprE)
BXH: BAXH7_01013(apr)
BQY: MUS_1081(aprE)
BAMI: KSO_014610
BAMC: U471_10430
BAMF: U722_05330
BCX: BCA_4942
BTL: BALH_4378
BPU: BPUM_0972
BMH: BMWSH_p211(alp)
BMEG: BG04_5989
BJS: MY9_1131
BACP: SB24_04625
BACB: OY17_07935
BACY: QF06_04075
BACL: BS34A_11440(aprE)
BALM: BsLM_1072
BGY: BGLY_1146(apr) BGLY_1970
BHA: BH0684(alp) BH0855
BCL: ABC0761(aprE)
GTN: GTNG_3101
LSP: Bsph_0341
HLI: HLI_15035
PASA: BAOM_2408(aprE)
PSYO: PB01_03765
ESI: Exig_1251
EAN: Eab7_1202
PPM: PPSC2_00675(epr)
PPO: PPM_0127(epr)
PPQ: PPSQR21_001320(aprE)
PPOY: RE92_11030
PMW: B2K_36240
PSAB: PSAB_00510
PRI: PRIO_0115 PRIO_6716(aprE)
PSWU: SY83_18965
ASOC: CB4_03352(aprE)
SIV: SSIL_3520
CTH: Cthe_3137
EAC: EAL2_808p03370(epr)
STH: STH1033
HMO: HM1_2600
MTHO: MOTHE_c20730(aprE)
MTHZ: MOTHA_c21500(aprE)
TOC: Toce_0485
LPIL: LIP_0524
ROP: ROP_55190
RRT: 4535765_02483(aprE)
GBR: Gbro_2515
TPR: Tpau_1297
SBH: SBI_04305
SVE: SVEN_0531
STRM: M444_28920
TCU: Tcur_1456
SEN: SACE_3537
PSEA: WY02_07925
PAUT: Pdca_21980
ALO: CRK57421
ASE: ACPL_4119(aprA)
ACTN: L083_4229
ACTS: ACWT_3990
CYT: cce_0328
NAZ: Aazo_1099
DOU: BMF77_00947(apr)
RCA: Rcas_2539
TRO: trd_1703
TSC: TSC_c03630(apr1)
TAQ: TO73_2195
WCH: wcw_1929(aprE)
PLS: VT03_06235(aprN)
GES: VT84_14990(apr_1) VT84_17225(aprN)
FSC: FSU_1274
PMUC: ING2E5A_2610(aprN)
PSAC: PSM36_1910
FAE: FAES_2745 FAES_3048(aprE)
PAA: Paes_2280
FPL: Ferp_2094
THS: TES1_1967
PPAC: PAP_01675
MBAK: MSBR3_1511
MTHR: MSTHT_0610
MTHE: MSTHC_0110
MHOR: MSHOH_1113
MPY: Mpsy_0077
MPD: MCP_1283
HME: HFX_5138(aprE) HFX_5181(aprE)
HLA: Hlac_2196
HDF: AArcSl_0415(aprE)
HTU: Htur_0058
NMG: Nmag_1874
 » show all
Reference
1
  Authors
Ottesen, M. and Svendsen, I.
  Title
The subtilisins.
  Journal
Methods Enzymol 19:199-215 (1970)
Reference
2
  Authors
Markland, F.S. and Smith, E.L.
  Title
Subtilisins: primary structure, chemical and physical properties.
  Journal
In: Boyer, P.D. (Ed.), The Enzymes, 3rd ed., vol. 3, Academic Press, New York, 1971, p. 561-608.
Reference
3  [PMID:6221910]
  Authors
Tang H.
  Title
[The use of single-dose total body irradiation before bone marrow transplantation in treatment of leukemia]
  Journal
Zhonghua Fang She Xue Za Zhi 16:296-300 (1982)
Reference
4  [PMID:3927935]
  Authors
Nedkov P, Oberthur W, Braunitzer G.
  Title
Determination of the complete amino-acid sequence of subtilisin DY and its comparison with the primary structures of the subtilisins BPN', Carlsberg and amylosacchariticus.
  Journal
Biol Chem Hoppe Seyler 366:421-30 (1985)
DOI:10.1515/bchm3.1985.366.1.421
Reference
5  [PMID:3108260]
  Authors
Ikemura H, Takagi H, Inouye M.
  Title
Requirement of pro-sequence for the production of active subtilisin E in Escherichia coli.
  Journal
J Biol Chem 262:7859-64 (1987)
  Sequence
[bsu:BSU10300]
Reference
6
  Authors
Polgar, L.
  Title
Structure and function of serine proteases.
  Journal
In: Neuberger, A. and Brocklehurst, K. (Eds.), New Comprehensive Biochemistry: Hydrolytic Enzymes, vol. 16, Elsevier, Amsterdam, 1987, p. 159-200.
Other DBs
ExplorEnz - The Enzyme Database: 3.4.21.62
IUBMB Enzyme Nomenclature: 3.4.21.62
ExPASy - ENZYME nomenclature database: 3.4.21.62
BRENDA, the Enzyme Database: 3.4.21.62
CAS: 9014-01-1

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