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Information on EC 3.4.21.62 - Subtilisin and Organism(s) Bacillus amyloliquefaciens and UniProt Accession P00782
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3.4.21.62 SubtilisinSpecify your search results
Word Map
- 3.4.21.62
- hydrolysates
- chymotrypsin
- prion
- elastase
- papain
- sds
- aeruginosa
- prpsc
- proteinases
- casein
- staphylococcus
- proprotein
- pronase
-
convertase
- alpha-chymotrypsin
- scrapie
- dnase
-
ultrafiltration
-
proteinaceous
-
spongiform
- thermolysin
- pmsf
-
bacteriocins
- licheniformis
- propeptide
-
paraffin-embedded
- gelatin
-
protease-resistant
-
formalin-fixed
- pcsk9
- alpha-amylase
-
cytotoxin
-
boil
- creutzfeldt-jakob
-
phenylmethylsulfonyl
- amyloliquefaciens
- pumilus
- bromelain
-
alkaliphilic
-
shiga
-
i-converting
-
transesterification
- furin
- album
-
defatted
- prodomain
- pancreatin
- p-nitroanilide
-
kazal
- detergent
- industry
- biotechnology
- food industry
- medicine
- synthesis
- degradation
- analysis
The taxonomic range for the selected organisms is: Bacillus amyloliquefaciens
The enzyme appears in selected viruses and cellular organisms
The enzyme appears in selected viruses and cellular organisms
Reaction Schemes
Hydrolysis of proteins with broad specificity for peptide bonds, and a preference for a large uncharged residue in P1. Hydrolyses peptide amides
Synonyms
proteinase k, subtilisin, alkaline protease, alcalase, subtilisin carlsberg, subtilase, subtilisin-like protease, savinase, alkaline serine protease, subtilisin a, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
Alcalase
-
-
-
-
Alcalase 0.6L
-
-
-
-
Alcalase 2.5L
-
-
-
-
ALK-enzyme
-
-
-
-
Alkaline mesentericopeptidase
-
-
-
-
Alkaline protease
-
-
-
-
Bacillopeptidase A
-
-
-
-
Bacillopeptidase B
-
-
-
-
Bacillus subtilis alkaline proteinase Bioprase
-
-
-
-
Bioprase AL 15
-
-
-
-
Bioprase APL 30
-
-
-
-
Colistinase
-
-
-
-
Esperase
-
-
-
-
Genenase I
-
-
-
-
Kazusase
-
-
-
-
Maxatase
-
-
-
-
Nagarse
-
-
-
-
Opticlean
-
-
-
-
Orientase 10B
-
-
-
-
Peptidase, subtilo-, A
-
-
-
-
Protease S
-
-
-
-
Protease VIII
-
-
-
-
Protease XXVII
-
-
-
-
Proteinase, Bacillus subtilis alkaline
-
-
-
-
Protin A 3L
-
-
-
-
Savinase
-
-
-
-
Savinase 16.0L
-
-
-
-
Savinase 32.0 L EX
-
-
-
-
Savinase 4.0T
-
-
-
-
Savinase 8.0L
-
-
-
-
SP 266
-
-
-
-
Subtilisin amylosacchariticus
-
from Bacillus subtilis var. amylosacchariticus
Subtilisin E
-
-
-
-
Subtilisin GX
-
-
-
-
Subtilisin Novo
-
-
-
-
Subtilisin S41
-
-
-
-
Subtilisin Sendai
-
-
-
-
Subtilopeptidase
-
-
-
-
Superase
-
-
-
-
Thermoase
-
-
-
-
Thermoase PC 10
-
-
-
-
additional information
additional information
-
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
additional information
-
synonyms of subtilisin Carlsberg: subtilisin, subtilisin A, subtilopeptidase A, alcalase Novo, synonyms of subtilisin BPN': nagarse proteinase, Nagarse, BPN', subtilopeptidase C, synonyms of subtilisin Novo: bacterial proteinase Novo, subtilisin B, subtilopeptidase B
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Hydrolysis of proteins with broad specificity for peptide bonds, and a preference for a large uncharged residue in P1. Hydrolyses peptide amides
hydrolysis of proteins with broad specificity for peptide bonds, and a preference for a large uncharged residue in P1. Hydrolyzes peptide amides. Mechanism
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of peptide bond
-
-
-
-
ester bond hydrolysis
-
-
-
-
transpeptidation
-
-
-
-
transesterification
-
-
-
-
CAS REGISTRY NUMBER
COMMENTARY
9014-01-1
-
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
casein + H2O
?
-
caseinolytic activity is determined using the casein plate method
-
-
?
Human fibrinogen + H2O
?
-
fibrinolytic activity is determined using the fibrin plate method
-
-
?
N-Succ-Ala-Ala-Pro-Phe-4-nitroanilide + H2O
N-Succ-Ala-Ala-Pro-Phe + 4-nitroaniline
-
-
-
-
?
succinyl-Ala-Ala-Pro-Phe 4-nitroanilide + H2O
succinyl-Ala-Ala-Pro-Phe + 4-nitroaniline
-
-
-
-
?
succinyl-L-Ala-L-Ala-L-Phe-7-amido-4-methylcoumarin + H2O
succinyl-L-Ala-L-Ala-L-Phe + 7-amino-4-methylcoumarin
-
-
-
-
?
succinyl-L-Ala-L-Ala-L-Pro-Gly-4-nitroanilide + H2O
succinyl-L-Ala-L-Ala-L-Pro-Gly + 4-nitroaniline
-
-
-
-
?
succinyl-L-Ala-L-Ala-L-Pro-L-Ala-4-nitroanilide + H2O
succinyl-L-Ala-L-Ala-L-Pro-L-Ala + 4-nitroaniline
-
-
-
-
?
succinyl-L-Ala-L-Ala-L-Pro-L-Lys-4-nitroanilide + H2O
succinyl-L-Ala-L-Ala-L-Pro-L-Lys + 4-nitroaniline
-
-
-
-
?
succinyl-L-Ala-L-Ala-L-Pro-L-Met-4-nitroanilide + H2O
succinyl-L-Ala-L-Ala-L-Pro-L-Met + 4-nitroaniline
-
-
-
-
?
succinyl-L-Ala-L-Ala-L-Pro-L-Phe-4-nitroanilide + H2O
succinyl-L-Ala-L-Ala-L-Pro-L-Phe + 4-nitroaniline
-
-
-
-
?
succinyl-L-Ala-L-Ala-L-Pro-L-Tyr-4-nitroanilide + H2O
succinyl-L-Ala-L-Ala-L-Pro-L-Tyr + 4-nitroaniline
-
-
-
-
?
succinyl-L-Asp-L-Val-L-Arg-L-Ala-L-Phe-7-amido-4-methylcoumarin + H2O
succinyl-L-Asp-L-Val-L-Arg-L-Ala-L-Phe + 7-amino-4-methylcoumarin
-
-
-
-
?
additional information
?
-
-
reactions catalyzed: 1. peptide bond hydrolysis, 2. ester bond hydrolysis, 3. transesterification, 4. transpeptidation
-
-
?
additional information
?
-
-
reactions catalyzed: 1. peptide bond hydrolysis, 2. ester bond hydrolysis, 3. transesterification, 4. transpeptidation
-
-
?
additional information
?
-
-
alteration of substrate specificity by protein engineering
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Ca2+
-
stabilizing mutations are usually calcium-dependent in their stabilizing effect
additional information
-
metal ion sites are not formed until late in folding and do not influence the kinetics of folding to the intermediate complex
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
fungal protease inhibitor F
-
specific inhibitor toward subtilisin-type protease. P1 residue most signficantly affects inhibitory specificity. Mutant T29M has stronger subtilisin-inhibitory activity than the wild-type, mutants T29E and T29R are relatively weaker inhibitors. Inhibitory activities of mutants T29F and T29L are as strong as that of the wild-type
-
Inhibitor of Amaranthus caudatus seeds
-
subtilisin Novo (BPN') from Bacillus amyloliquefaciens, subtilisin Carlsberg from Bacillus licheniformis
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
-
prodomain mutant proR9 accelerates subtilisin folding. Subtilisin folding with the wild-type prodomain is slow. The wild-type prodomain binds 100times slower than proR9
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.15
MeO-succinyl-Ala-Ala-Phe 4-nitroanilide
-
succinyl-Ala-Ala-Pro-Phe 4-nitroanilide, subtilisin BPN'
0.13
succinyl-Ala-Ala-Pro-Phe 4-nitroanilide
-
mutant subtilisin BPN' Asp to Ser99
0.36
succinyl-L-Ala-L-Ala-L-Phe-7-amido-4-methylcoumarin
-
mutant Y217L, pH 8.3, 25°C
0.45
succinyl-L-Ala-L-Ala-L-Pro-L-Phe-4-nitroanilide
-
mutant Y217L, pH 8.3, 25°C
0.33
succinyl-L-Asp-L-Val-L-Arg-L-Ala-L-Phe-7-amido-4-methylcoumarin
-
mutant Y217L, pH 8.3, 25°C
0.15
N-Succ-Ala-Ala-Pro-Phe-4-nitroanilide
-
pH 7.4, 37°C, mutant S101W/G169A/V192A
0.35
N-Succ-Ala-Ala-Pro-Phe-4-nitroanilide
-
pH 7.4, 37°C, wild-type
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
6.4
succinyl-L-Ala-L-Ala-L-Phe-7-amido-4-methylcoumarin
-
mutant Y217L, pH 8.3, 25°C
210
succinyl-L-Ala-L-Ala-L-Pro-L-Phe-4-nitroanilide
-
mutant Y217L, pH 8.3, 25°C
68
succinyl-L-Asp-L-Val-L-Arg-L-Ala-L-Phe-7-amido-4-methylcoumarin
-
mutant Y217L, pH 8.3, 25°C
231.3
N-Succ-Ala-Ala-Pro-Phe-4-nitroanilide
-
pH 7.4, 37°C, wild-type
586.2
N-Succ-Ala-Ala-Pro-Phe-4-nitroanilide
-
pH 7.4, 37°C, mutant S101W/G169A/V192A
45
succinyl-Ala-Ala-Pro-Phe 4-nitroanilide
-
mutant subtilisin BPN' Asp99Ser
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
660
N-Succ-Ala-Ala-Pro-Phe-4-nitroanilide
-
pH 7.4, 37°C, wild-type
3910
N-Succ-Ala-Ala-Pro-Phe-4-nitroanilide
-
pH 7.4, 37°C, mutant S101W/G169A/V192A
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.000000017
chymotrypsin inhibitor 2 mutant M59A, chymotrypsin inhibitor 2 mutant M59F
-
-
-
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
-
alteration of pH-profile by protein engineering
additional information
-
mutant subtilisin Asp to Ser99, change of just one surface charge which is 14-15 A from the active site of subtilisin has a significant effect on the pH-dependence
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
-
characterization of a folding intermediate
additional information
-
amino acid composition of: subtilisin BPN'
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
1.8 A resolution structure of an inactive form (by replacing the catalytic nucleophile Ser 221 with alanine) of the protease subtilisin S189, in complex with azide and with a prodomain substrate that spans the active site. The substrate is well ordered across the active site, and the azide anion is observed bound adjacent to Ala 32. Although S189, like wild-type subtilisin, has Ser as the catalytic nucleophile at residue 221, these crystal structures have Ala 221 to prevent cleavage of the substrate
in complex with chymotrypsin inhibitor 2 and its mutants M59K, M59Y, M59F, M59A, M59G, Y61A
-
wild-type and thermostable mutant 7150 subtilisin at 1.8 A resolution
-
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
A1C
does not change the catalytic properties of subtilisin S189 but allows the introduction of a fluorescent group at its N-terminus
D32A
engineered variant of the protease subtilisin, denoted S189, mutation renders the enzyme's activity dependent on the presence of certain small anions such as fluoride or azide. Is activated more than 3000fold by azide
G169A
L126I
M50F
N218S
N76D
Q271E
S101W/G169A/V192A
-
mutant shows 1.4fold activity compared to wild-type, kcat doubled compared to wild-type, Km decreased compared to wild-type
S188P
S194P
S221A
-
a delta75-83 mutant. Shows slow folding reaction. Is unstable at low metal concentration, unfolding at a rate of 0.6 h-1. If denatured, it is refolded with an excess of proR9
S221C
T22C/S87C/S221C
-
if denatured, it is refolded with an excess of proR9. About 75% is rapidly bound to proR9. 25% undergoes a slow step prior to binding
T254A
Y217K
additional information
L126I
-
site-directed mutagenesis, BPN', stable only in presence of excess Ca2+
M50F
-
site-directed mutagenesis, BPN',stabilized in EDTA, but destabilized slightly in CaCl2
N218S
-
site-directed mutagenesis, BPN', stabilized significantly, either with or without Ca2+
Q271E
-
site-directed mutagenesis, BPN', stabilized significantly, either with or without Ca2+
S188P
-
site-directed mutagenesis, BPN', stable only in presence of excess Ca2+
T254A
-
site-directed mutagenesis, BPN', stable only in presence of excess Ca2+
Y217K
-
site-directed mutagenesis, BPN', stabilized significantly, either with or without Ca2+
additional information
-
introduction of about 20 site-directed mutations to obtain a variant with increased sequence selectivity, a predomain that can direct cleavage to the junction of any protein fused to it, and a modified active site to kinetically isolate binding and cleavage reactions. Identification of specific anions that trigger the processing reaction so that column-immobilized mutant enzyme can be used as both the affinity ligand and the processing protease for one-step purification methods
additional information
-
sequential randomization of 12 amino acid positions in calcium-free enzyme. Mutations increase the half-life of enzyme at elevated temperature by 15000fold and partially increase ratio of kcat/KM-value
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
4 - 12
-
enzyme loses its activity at pH lower 4, retains 60% of its activity at pH higher 12
717697
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
65
-
pH 8.0, 10 mM CaCl2, half-life of wild-type enzyme: 59 min, half-life of mutant 7150 enzyme: 223 min
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
Alteration of stability to oxidative, thermal and alkaline inactivation by protein engineering
-
stability is a property of subtilisin which has proven particularly amenable to enhancement via random mutagenesis
-
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
almost every property of subtilisin has been altered by protein engineering, e.g. substrate specificity, pH-profile and stability to oxidative, thermal and alkaline inactivation
-
Bacillus amyloliquefaciens gene expressed in Bacillus subtilis I-168 (Marburg strain)
-
expressed in the protease deficient host Bacillus subtilis ISW1214
-
in vivo formation and stability of engineered disulfide bonds in subtilisin
-
inactive mutants of subtilisin BPN expressed in Bacillus subtilis. Expression of prodomain mutant proR9 in Escherichia coli strain BL21(DE3)
-
subtilisin 7150, mutagenized subtilisin with enhanced thermal stability
-
subtilisin BPN' cloned, sequenced and expressed at high levels from its natural promoter sequences in Bacillus subtilis
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
-
slow folding of subtilisin results from the formation of an unstable and topologically challenged intermediate and the proline-limited isomerization of the intermediate to the native state
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Ottesen, M.; Svendsen, I.
The subtilisins
Methods Enzymol.
19
199-215
1970
Bacillus amyloliquefaciens, Bacillus subtilis, Bacillus sp. (in: Bacteria)
-
Kraut, J.
Subtilisin: X-ray structure
The Enzymes, 3rd Ed. (Boyer, P. D. , ed. )
3
547-560
1971
Bacillus amyloliquefaciens, Bacillus sp. (in: Bacteria)
-
Markland, F.S.; Smith, E.L.
Subtilisins: primary structure, chemical and physical properties
The Enzymes, 3rd Ed. (Boyer, P. D. , ed. )
3
561-608
1971
Bacillus amyloliquefaciens, Bacillus sp. (in: Bacteria)
-
Nedkov, P.; Oberthur, W.; Braunitzer, G.
Determination of the complete amino-acid sequence of subtilisin DY and its comparison with the primary structures of the subtilisins BPN, Carlsberg and amylosacchariticus
Biol. Chem. Hoppe-Seyler
366
421-430
1985
Bacillus amyloliquefaciens, Bacillus subtilis, Bacillus sp. (in: Bacteria), Bacillus subtilis DY
Wells, J.A.; Estell, D.A.
Subtilisin - an enzyme designed to be engineered
Trends Biochem. Sci.
13
291-297
1988
Bacillus amyloliquefaciens
Bodhe, A.M.
Purification and properties of a subtilisin inhibitor and an associated trypsin inhibitor from Dolichos biflorus
Biochim. Biophys. Acta
1073
11-17
1991
Bacillus amyloliquefaciens
Wells, J.A.; Powers, D.B.
In vivo formation and stability of engineered disulfide bonds in subtilisin
J. Biol. Chem.
261
6564-6570
1986
Bacillus amyloliquefaciens
Hejgaard, J.; Dam, J.; Peterson, L.C.; Bjorn, S.E.
Primary structure and specificity of the major serine proteinase inhibitor of amaranth (Amaranthus caudatus L.) seeds
Biochim. Biophys. Acta
1204
68-74
1994
Bacillus amyloliquefaciens, Bacillus licheniformis, Bacillus sp. (in: Bacteria)
Eder, J.; Rheinnecker, M.; Fersht, A.R.
Folding of subtilisin BPN: characterization of a folding intermediate
Biochemistry
32
18-26
1993
Bacillus amyloliquefaciens, Bacillus subtilis, Bacillus sp. (in: Bacteria), Bacillus subtilis DB104
Bryan, P.N.; Rollence, M.L.; Pantoliano, M.W.; Wood, J.; Finzel, B.C.; Gilliland, G.L.; Howard, A.J.; Poulos, T.L.
Proteases of enhanced stability: characterization of a thermostable variant of subtilisin
Proteins Struct. Funct. Genet.
1
326-334
1986
Bacillus amyloliquefaciens
Thomas, P.G.; Russell, A.J.; Fersht, A.R.
Tailoring the pH dependence of enzyme catalysis using protein engineering
Nature
318
375-376
1985
Bacillus amyloliquefaciens, Bacillus sp. (in: Bacteria)
-
Wells, J.A.; Ferrari, E.; Henner, D.J.; Estell, D.A.; Chen, E.Y.
Cloning, sequencing, and secretion of Bacillus amyloliquefaciens subtilisin in Bacillus subtilis
Nucleic Acids Res.
11
7911-7925
1983
Bacillus amyloliquefaciens
Alexander, P.A.; Ruan, B.; Strausberg, S.L.; Bryan, P.N.
Stabilizing mutations and calcium dependent stability of subtilisin
Biochemistry
40
10640-10644
2001
Bacillus amyloliquefaciens
Bryan, P.N.
Protein engineering of subtilisin
Biochim. Biophys. Acta
1543
203-222
2000
Bacillus amyloliquefaciens, Bacillus sp. (in: Bacteria)
Radisky, E.S.; Kwan, G.; Karen Lu, C.J.; Koshland, D.E.
Binding, proteolytic, and crystallographic analyses of mutations at the protease-inhibitor interface of the subtilisin BPN/chymotrypsin inhibitor 2 complex
Biochemistry
43
13648-13656
2004
Bacillus amyloliquefaciens
Ruan, B.; Fisher, K.E.; Alexander, P.A.; Doroshko, V.; Bryan, P.N.
Engineering subtilisin into a fluoride-triggered processing protease useful for one-step protein purification
Biochemistry
43
14539-14546
2004
Bacillus amyloliquefaciens
Strausberg, S.L.; Ruan, B.; Fisher, K.E.; Alexander, P.A.; Bryan, P.N.
Directed coevolution of stability and catalytic activity in calcium-free subtilisin
Biochemistry
44
3272-3279
2005
Bacillus amyloliquefaciens
Almog, O.; Kogan, A.; de Leeuw, M.; Gdalevsky, G.Y.; Cohen-Luria, R.; Parola, A.H.
Structural insights into cold inactivation of tryptophanase and cold adaptation degrees of subtilisin S41: Minireview
Biopolymers
89
354-359
2008
Bacillus subtilis, Bacillus licheniformis, Lysinibacillus sphaericus, Bacillus amyloliquefaciens (P00782), Vibrio sp. (Q8GB52), Bacillus subtilis TA41
Fisher, K.E.; Ruan, B.; Alexander, P.A.; Wang, L.; Bryan, P.N.
Mechanism of the kinetically-controlled folding reaction of subtilisin
Biochemistry
46
640-651
2007
Bacillus amyloliquefaciens
Taniguchi, M.; Atiwetin, P.; Hirai, T.; Itoh, M.; Harada, S.; Hara, S.; Kamei, K.
Interaction of subtilisin BPN and recombinant fungal protease inhibitor F from silkworm with substituted P1 site residues
Biosci. Biotechnol. Biochem.
70
1262-1264
2006
Bacillus amyloliquefaciens
Gallagher, T.; Ruan, B.; London, M.; Bryan, M.A.; Bryan, P.N.
Structure of a switchable subtilisin complexed with a substrate and with the activator azide
Biochemistry
48
10389-10394
2009
Bacillus amyloliquefaciens (P00782), Bacillus amyloliquefaciens
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