KEGG   ENZYME: 3.4.21.100Help
Entry
EC 3.4.21.100               Enzyme                                 

Name
sedolisin;
Pseudomonas sp. pepstatin-insensitive carboxyl proteinase;
pseudomonapepsin;
pseudomonalisin;
sedolysin
Class
Hydrolases;
Acting on peptide bonds (peptidases);
Serine endopeptidases
BRITE hierarchy
Reaction(IUBMB)
Hydrolysis of the B chain of insulin at -Glu13!Ala-, -Leu15!Tyr- and -Phe25!Tyr-, and angiotensin I at -Tyr4!Ile-. A good synthetic substrate is Lys-Pro-Ile-Glu-Phe!Phe(NO2)-Arg-Leu.
Comment
An enzyme secreted by Pseudomonas sp. No. 101. Optimum pH is 4. It is distinguished from xanthomonapepsin by its insensitivity to EPNP and from scytalidopepsin B by this property and by its unrelated amino-acid sequence. Inhibited by tyrostatin, a peptide aldehyde [2]. Type example of peptidase family S53.
History
EC 3.4.21.100 created 1995 as EC 3.4.23.37, transferred 2001 to EC 3.4.21.100, modified 2003
Orthology
K05998  pseudomonalisin
Genes
XAL: XALC_1198
DJA: HY57_08615
DTX: ATSB10_19690
CVI: CV_1965 CV_1968
CVC: BKX93_23225 BKX93_23230
CHRO: CXB49_09385 CXB49_12540 CXB49_12545
RIN: ACS15_5322
BMA: BMA1538 BMAA0435
BMV: BMASAVP1_A2037
BML: BMA10229_A3274
BMAL: DM55_186(pcp)
BMAE: DM78_1853(pcp)
BMAQ: DM76_166(pcp)
BMAF: DM51_1239(pcp) DM51_4158
BMAZ: BM44_1815(pcp) BM44_3273
BMAB: BM45_1377(pcp) BM45_4111
BPSE: BDL_3405(pcp) BDL_5091(pcp)
BPSM: BBQ_1194(pcp) BBQ_4404(pcp)
BPSU: BBN_1320(pcp) BBN_5191(pcp)
BPSD: BBX_1806(pcp) BBX_4257(pcp)
BPK: BBK_2822(pcp) BBK_4455(pcp)
BPSH: DR55_2441(pcp) DR55_3532(pcp)
BPSA: BBU_19(pcp) BBU_4289(pcp)
BPSO: X996_2028(pcp) X996_5809(pcp)
BUT: X994_446(pcp) X994_5370(pcp)
BTQ: BTQ_1866(pcp) BTQ_3938(pcp)
BTJ: BTJ_489(pcp) BTJ_4970(pcp)
BTZ: BTL_1729(pcp) BTL_3439(pcp)
BTD: BTI_4244(pcp)
BTV: BTHA_1883(pcp) BTHA_4447(pcp)
BTHE: BTN_3039(pcp) BTN_5425(pcp)
BTHM: BTRA_2009(pcp) BTRA_5700(pcp)
BTHL: BG87_1953(pcp) BG87_3393(pcp)
BOK: DM82_1726(pcp) DM82_5981(pcp)
BOC: BG90_2994(pcp) BG90_4659(pcp)
BVE: AK36_4409(pcp)
BCEN: DM39_3999(pcp)
BCEW: DM40_3906(pcp) DM40_3931(pcp)
BAM: Bamb_3301
BMU: Bmul_4660
BMK: DM80_3859(pcp)
BMUL: NP80_3915(pcp)
BCED: DM42_4129(pcp) DM42_4164(pcp)
BDL: AK34_4498(pcp)
BUB: BW23_4683(pcp)
BPSL: WS57_09010
BSTG: WT74_23965
BGU: KS03_5159(pcp)
BGO: BM43_5602(pcp)
BUK: MYA_4042
BUL: BW21_3784(pcp)
CFU: CFU_2834
CPRA: CPter91_0553(pcp) CPter91_1734(pcp) CPter91_2251(pcp)
 » show all
Taxonomy
Reference
1  [PMID:3548827]
  Authors
Oda K, Sugitani M, Fukuhara K, Murao S.
  Title
Purification and properties of a pepstatin-insensitive carboxyl proteinase from a gram-negative bacterium.
  Journal
Biochim. Biophys. Acta. 923 (1987) 463-9.
Reference
2  [PMID:1562589]
  Authors
Oda K, Nakatani H, Dunn BM.
  Title
Substrate specificity and kinetic properties of pepstatin-insensitive carboxyl proteinase from Pseudomonas sp. No. 101.
  Journal
Biochim. Biophys. Acta. 1120 (1992) 208-14.
Reference
3  [PMID:11323721]
  Authors
Wlodawer A, Li M, Dauter Z, Gustchina A, Uchida K, Oyama H, Dunn BM, Oda K.
  Title
Carboxyl proteinase from Pseudomonas defines a novel family of subtilisin-like enzymes.
  Journal
Nat. Struct. Biol. 8 (2001) 442-6.
  Sequence
Reference
4  [PMID:12673349]
  Authors
Wlodawer A, Li M, Gustchina A, Oyama H, Dunn BM, Oda K.
  Title
Structural and enzymatic properties of the sedolisin family of serine-carboxyl peptidases.
  Journal
Acta. Biochim. Pol. 50 (2003) 81-102.
Other DBs
ExplorEnz - The Enzyme Database: 3.4.21.100
IUBMB Enzyme Nomenclature: 3.4.21.100
ExPASy - ENZYME nomenclature database: 3.4.21.100
BRENDA, the Enzyme Database: 3.4.21.100
CAS: 848318-58-1

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