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Information on EC 3.4.21.81 - Streptogrisin B and Organism(s) Streptomyces griseus and UniProt Accession P00777

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EC Tree
     3 Hydrolases
         3.4 Acting on peptide bonds (peptidases)
             3.4.21 Serine endopeptidases
                3.4.21.81 Streptogrisin B
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This record set is specific for:
Streptomyces griseus
UNIPROT: P00777 not found.
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Word Map
The taxonomic range for the selected organisms is: Streptomyces griseus
The enzyme appears in selected viruses and cellular organisms
Reaction Schemes
Hydrolysis of proteins with trypsin-like specificity
Synonyms
proteinase b, protease b, streptomyces griseus protease b, streptomyces griseus proteinase b, pronase b, streptogrisin b, streptomyces griseus peptidase b, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Pronase B
-
-
-
-
Proteinase B
-
-
Proteinase, Streptomyces griseus serine B
-
-
-
-
Serine proteinase B
-
-
-
-
Streptogrisin B
-
-
Streptomyces griseus peptidase B
-
SGPB
Streptomyces griseus protease B
Streptomyces griseus proteinase 1
-
-
-
-
Streptomyces griseus proteinase B
-
-
-
-
additional information
-
a component of pronase, and a homologue of alpha-lytic endopeptidase, distinct from Streptomyces trypsin
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of peptide bond
CAS REGISTRY NUMBER
COMMENTARY hide
55071-87-9
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
3 acetyl-Pro-Ala-Phe-Phe-NH2 + H2O
acetyl-Pro-Ala-Phe-Phe + NH3 + acetyl-Pro-Ala + Phe-Phe-NH2 + acetyl-Pro-Ala-Phe + Phe-NH2
show the reaction diagram
-
hydrolyzed at the Ala-Phe, the Phe-Phe and the Phe-NH2 bond
-
-
?
acetyl-Ala-Ala-Tyr-4-methylcoumarin 7-amide + H2O
acetyl-Ala-Ala-Tyr + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
-
-
?
Acetyl-Pro-Ala-Ala-Phe-NH2 + H2O
?
show the reaction diagram
-
split at the amide bond as well as at the Ala-Ala bond
-
-
?
Acetyl-Pro-Ala-Gly-Phe-NH2 + H2O
?
show the reaction diagram
-
split at the amide bond as well as at the Ala-Gly bond
-
-
?
Acetyl-Pro-Ala-Leu-Phe-NH2 + H2O
Acetyl-Pro-Ala-Leu-Phe-OH + NH3
show the reaction diagram
-
hydrolyzed at the amide bond only
-
-
?
Acetyl-Pro-Ala-Pro-Phe-NH2 + H2O
Acetyl-Pro-Ala-Pro-Phe-OH + NH3
show the reaction diagram
-
hydrolyzed at the amide bond only
-
-
?
N-Acetyl-L-Pro-L-Leu-p-nitroanilide + H2O
?
show the reaction diagram
-
-
-
-
?
OMSVP3 + H2O
?
show the reaction diagram
-
ovomucoid third domain from silver pheasant, potent inhibitor of chymotrypsin, subtilisin, and elastase
cleavage between residues Met18-Glu19
-
?
OMSVP3 mutant P14C/N39C + H2O
?
show the reaction diagram
-
disulfide variant of the ovomucoid third domain from silver pheasant carrying an engineered Cys14-Cys39 bond near the reactive site
cleavage between residues Met18-Glu19. P14C/N39C can be selectively cleaved by Streptomyces griseus protease B at the reactive site of OMSVP3 to form a reactive site modified inhibitor. The conversion rate of P14C/N39C is much faster than that for wild type under any pH condition. The reactive site modified form of P14C/N39C is thermodynamically more stable than the intact one
-
?
Sc-AAPF-p-nitroanilide + H2O
?
show the reaction diagram
-
-
-
-
?
Sc-AAPF-SBn + FAASF-NH2
?
show the reaction diagram
-
-
ligation to nonapeptide by mutant S195A/T213L/F228H
-
?
Sc-AAPF-SBn + H2O
?
show the reaction diagram
-
-
-
-
?
Suc-AAPF-p-nitroanilide + H2O
?
show the reaction diagram
-
-
-
?
Suc-AAPF-SBzl + H2O
Suc-AAPF + phenylmethanethiol
show the reaction diagram
-
-
-
?
succinyl-Ala-Ala-Pro-4-methylcoumarin 7-amide + H2O
succinyl-Ala-Ala-Pro + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
-
-
?
succinyl-Ala-Ala-Pro-Phe 4-nitroanilide + H2O
succinyl-Ala-Ala-Pro-Phe + 4-nitroaniline
show the reaction diagram
-
-
-
-
?
succinyl-Ala-Ala-Pro-Phe-7-amido-4-methylcoumarin + H2O
succinyl-Ala-Ala-Pro-Phe + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
-
-
?
succinyl-Ala-Ala-Pro-X-4-nitroanilide + H2O
?
show the reaction diagram
-
-
-
?
succinyl-Ala-Ala-Pro-X-7-amido-4-methylcoumarin + H2O
?
show the reaction diagram
-
-
-
?
succinyl-L-Ala-L-Ala-L-Pro-L-Asp-4-nitroanilide + H2O
succinyl-L-Ala-L-Ala-L-Pro-L-Asp + 4-nitroaniline
show the reaction diagram
-
extremely poor substrate at pH 8 but becomes a moderately good substrate at pH 5.5
-
-
?
succinyl-L-Ala-L-Ala-L-Pro-L-Leu-4-nitroanilide + H2O
succinyl-L-Ala-L-Ala-L-Pro-L-Leu + 4-nitroaniline
show the reaction diagram
-
optimum at pH 7.5-8.0
-
-
?
succinyl-L-Ala-L-Ala-L-Pro-L-Lys-4-nitroanilide + H2O
succinyl-L-Ala-L-Ala-L-Pro-L-Lys + 4-nitroaniline
show the reaction diagram
-
optimum at pH 10.0
-
-
?
additional information
?
-
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
Bovine pancreatic trypsin inhibitor
-
Kunitz
-
N-tert-Butyloxycarbonyl-glycyl-L-leucyl-L-phenylalanine chloromethyl ketone
-
-
N-tert-Butyloxycarbonyl-L-alanylglycyl-L-phenylalanine chloromethyl ketone
-
-
protein inhibitor S13D14Y15-OMTKY3
a OMTKY3 mutant variant, recombinantly produced in Escherichia coli strain RV308 and purified, strong inhibition, overview
-
protein inhibitor S13D14Y15G18I19K21-OMTKY3
a OMTKY3 mutant variant, recombinantly produced in Escherichia coli strain RV308 and purified, strong inhibition, overview. S13D14Y15G18I19K21 OMTKY3 inhibits Streptomyces griseus protease B 10times more strongly than Streptomyces griseus protease A, EC 3.4.21.80
-
Soybean trypsin inhibitor
-
-
-
Squash inhibitor
-
-
-
Streptomyces subtilisin inhibitor
-
-
-
Third domain of the ovomucoid inhibitor from turkey
-
-
-
Turkey ovomucoid third domain
-
OMTKY3, inhibitor for serine peptidases
-
additional information
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.15
Acetyl-Ala-Ala-Tyr-4-methylcoumarin 7-amide
-
-
1.4
Acetyl-Pro-Ala-Leu-Phe-NH2
-
-
2.4
Acetyl-Pro-Ala-Pro-Phe-NH2
-
-
0.062 - 0.5
Suc-AAPF-p-nitroanilide
0.101
succinyl-Ala-Ala-Pro-Phe 4--nitroanilide
-
-
0.098
succinyl-Ala-Ala-Pro-Phe-7-amido-4-methylcoumarin
-
-
additional information
additional information
-
-
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.04
Acetyl-Ala-Ala-Tyr-4-methylcoumarin 7-amide
-
-
7.1
Acetyl-Pro-Ala-Leu-Phe-NH2
-
-
6.7
Acetyl-Pro-Ala-Pro-Phe-NH2
-
-
0.066 - 1884
Suc-AAPF-p-nitroanilide
153
succinyl-Ala-Ala-Pro-Phe 4-nitroanilide
-
-
3.3
succinyl-Ala-Ala-Pro-Phe-7-amido-4-methylcoumarin
-
-
additional information
additional information
-
-
-
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
740 - 10700
succinyl-L-Ala-L-Ala-L-Pro-L-Asp-4-nitroanilide
28200 - 25000000
succinyl-L-Ala-L-Ala-L-Pro-L-Leu-4-nitroanilide
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
10
-
substrate succinyl-L-Ala-L-Ala-L-Pro-L-Lys-4-nitroanilide
5.5 - 6
-
substrate succinyl-L-Ala-L-Ala-L-Pro-L-Asp-4-nitroanilide
6
-
hydrolysis reaction
7.5 - 8
-
substrate succinyl-L-Ala-L-Ala-L-Pro-L-Leu-4-nitroanilide
8.8 - 9.2
-
ligation reaction of mutant S195A/T213L/F228H
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
37
-
assay at
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
-
ratio of ligation to hydrolysis by mutant S195A/T213L/F228H decreases with increase in temperature from 30°C to 60°C
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
PRTB_STRGR
299
1
30554
Swiss-Prot
-
PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
18410
-
Streptomyces griseus, amino acid sequence
18412
-
1 * 18412, Streptomyces griseus, amino acid sequence
additional information
-
amino acid sequence of cysteic acid peptides from peptic digest
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
monomer
additional information
-
enzyme folds to native state that is thermodynamically marginally stable, apparent stability arises kinetically from unfolding free energy barriers. Enzyme has effective pro-regions to facilitate folding
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
-
enzyme has effective pro-regions to facilitate folding
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
bound to wild type OMTKY3 and to the Ala32I variant, by the hanging-drop vapor-diffusion method, SGPB and OMTKY3 Ala32I forms a 1 : 2 complex in the crystal
-
crystal structure in complex with turkey ovomucoid thir domain backbone variants OMTKY3-Pro18I and OMTKY3-psi[COO]-Leu18I
-
crystal structure of protease B with tripeptide chloromethyl ketone inhibitors
-
crystal structures of Leu18, Ala18, and Gly18 variants of turkey ovomucoid inhibitor third domain complexed with proteinase B
-
structure at 2.8 A resolution
-
structure of the complex of protease B with the third domain of the ovomucoid inhibitor from turkey at 1.8 A resolution
-
structure of the complex of proteinase B and polypeptide chymotrypsin inhibitor-1 from Russet Burbank potato tubers at 2.1 A resolution
-
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
S195A
-
active-site variant of protease B with peptide-ligation activity
S195A/T213L/F228H
-
i.e. streptoligase, catalyzes peptide ligation efficiently. Ligation proceeds via an acyl-enzyme intermediate involving H57. Mutant exhibits half-life for unfolding of 16.3 min at 55°C in the absence of stabilizing substrates
S195C
-
active-site variant of protease B with peptide-ligation activity
S195G
-
active-site variant of protease B with peptide-ligation activity
S195G/H57N
-
active-site variant of protease B with peptide-ligation activity
additional information
-
introduction of site-specific disulfide bonds into the flexible N-terminal loop of natural Kazal-type inhibitors to characterize the thermodynamics of the reactive site peptide bond hydrolysis. Mutant P14C/N39C is a disulfide variant of the ovomucoid third domain from silver pheasant carrying an engineered Cys14–Cys39 bond near the reactive site. The conversion rate of P14C/N39C by streptogrisin B is much faster than that for wild type under any pH condition
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
37 - 45
-
mutant S195A, completely inactivated in less than 1 min at 45°C, less than 20 min at 37°C
additional information
-
study of temperature-dependences of the folding and unfolding kinetics without enzyme pro region
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
Stable in presence of 6.0 M guanidinium chloride
-
ORGANIC SOLVENT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
guanidine-HCl
-
8 M, extremely stable
urea
-
6 M, extremely stable
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
further purification of a commercial preparation
mutants S195A and S195G
-
purified from a commercial preparation of Pronase
-
purified from Pronase
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
active-site variant genes clones in the Escherichia coli/Bacillus subtilis shuttle vector pEB-11 and expressed in Bacillus subtilis DB104
-
gene structure
-
genes constructed which encodes deletions at the amino-terminal end of the propeptide, deletions to the 76-amino-acid propeptide of SGPB cause an incremental loss in the production of the mature enzyme
-
RENATURED/Commentary
ORGANISM
UNIPROT
LITERATURE
study of temperature-dependencies of the folding and unfolding kinetics without enzyme pro region. Enzyme shows a maximal unfolding cooperativity and slow rate of global unfolding
-
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Henderson, G.; Krygsman, P.; Liu, C.J.; Davey, C.C.; Malek, L.T.
Characterization and structure of genes for proteases A and B from Streptomyces griseus
J. Bacteriol.
169
3778-3784
1987
Streptomyces griseus
Manually annotated by BRENDA team
Bauer, C.A.
Active centers of alpha-chymotrypsin and of Streptomyces griseus proteases 1 and 3. S2-P2 enzyme-substrate interactions
Eur. J. Biochem.
105
565-570
1980
Streptomyces griseus
Manually annotated by BRENDA team
Christensen, U.; Ishida, S.; Ishii, S.I.; Mitsui, Y.; Iitaka, Y.; McClarin, J.; Langridge, R.
Interactions of Streptomyces subtilisin inhibitor with Streptomyces griseus proteases A and B. Enzyme kinetic and computer simulation studies
J. Biochem.
98
1263-1274
1985
Streptomyces griseus
Manually annotated by BRENDA team
Greenblatt, H.M.; Ryan, C.A.; James, M.N.G.
Structure of the complex of Streptomyces griseus proteinase B and polypeptide chymotrypsin inhibitor-1 from Russet Burbank potato tubers at 2.1 A resolution
J. Mol. Biol.
205
201-228
1989
Streptomyces griseus
Manually annotated by BRENDA team
Jurasek, L.; Fackre, D.; Smillie, L.B.
Remarkable homology about the disulfide bridges of a trypsin-like enzyme from Streptomyces griseus
Biochem. Biophys. Res. Commun.
37
99-105
1969
Streptomyces griseus
Manually annotated by BRENDA team
Fujinaga, M.; Read, R.J.; Sielecki, A.; Ardelt, W.; Laskowski, M.; James, M.N.G.
Refined crystal structure of the molecular complex of Streptomyces griseus protease B, a serine protease, with the third domain of the ovomucoid inhibitor from turkey
Proc. Natl. Acad. Sci. USA
79
4868-4872
1982
Streptomyces griseus
Manually annotated by BRENDA team
Read, R.J.; Fujinaga, M.; Sielecki, A.R.; James, M.N.G.
Structure of the complex of Streptomyces griseus protease B and the third domain of the turkey ovomucoid inhibitor at 1.8-A resolution
Biochemistry
22
4420-4433
1983
Streptomyces griseus
Manually annotated by BRENDA team
Jurasek, L.; Carpenter, M.R.; Smillie, L.B.; Gertler, A.; Levy, S.; Ericsson, L.H.
Amino acid sequence of Streptomyces griseus protease B, A MAJOR COMPONENT OF Pronase
Biochem. Biophys. Res. Commun.
61
1095-1100
1974
Streptomyces griseus
Manually annotated by BRENDA team
Otlewski, J.; Zbyryt, T.; Krokoszynska, I.; Wilusz, T.
Inhibition of serine proteinases by squash inhibitors
Biol. Chem. Hoppe-Seyler
371
589-594
1990
Streptomyces griseus
Manually annotated by BRENDA team
Delbaere, D.T.J.; Brayer, G.D.; James, M.N.G.
The 2.8 A resolution structure of Streptomyces griseus protease B and its homology with alpha-chymotrypsin and Streptomyces griseus protease A
Can. J. Biochem.
57
135-144
1979
Streptomyces griseus
Manually annotated by BRENDA team
James, M.N.G.; Brayer, G.D.; Delbaere, L.T.J.; Sielecki, A.R.
Crystal structure studies and inhibition kinetics of tripeptide chloromethyl ketone inhibitors with Streptomyces griseus protease B
J. Mol. Biol.
139
423-438
1980
Streptomyces griseus
Manually annotated by BRENDA team
Huang, K.; Wuyuan, L.; Anderson, S.; Laskowski, M.; James, M.N.G.
Water molecules participate in proteinase-inhibitor interactions: crystal structures of Leu18, Ala18, and Gly18 variants of turkey ovomucoid inhibitor third domain complexed with Streptomyces griseus proteinase B
Protein Sci.
4
1985-1997
1995
Streptomyces griseus
Manually annotated by BRENDA team
Johnson, E.R.; Lamkin, R.M.; Jordan, K.J.; Gordon, J.A.; Lindley, B.R.
Determination of the cleavage specificity of Streptomyces griseus protease B in the presence of guanidinium chloride
Int. J. Pept. Protein Res.
30
170-176
1987
Streptomyces griseus
Manually annotated by BRENDA team
Bauer, C.A.
Purity and pH-dependence of Streptomyces griseus protease 1
Acta Chem. Scand. B
31
637-639
1977
Streptomyces griseus
Manually annotated by BRENDA team
Elliott, R.J.; Bennet, A.J.; Braun, C.A.; MacLeod, A.M.; Borgford, T.J.
Active-site variants of Streptomyces griseus protease B with peptide-ligation activity
Chem. Biol.
7
163-171
2000
Streptomyces griseus
Manually annotated by BRENDA team
Baardsnes, J.; Sidhu, S.; MacLeod, A.; Elliott, J.; Morden, D.; Watson, J.; Borgford, T.
Streptomyces griseus protease B: secretion correlates with the length of the propeptide
J. Bacteriol.
180
3241-3244
1998
Streptomyces griseus
Manually annotated by BRENDA team
Bateman, K.S.; Huang, K.; Anderson, S.; Lu, W.; Qasim, M.A.; Laskowski, M.Jr.; James, M.N.
Contribution of peptide bonds to inhibitor-protease binding: crystal structures of the turkey ovomucoid third domain backbone variants OMTKY3-Pro18I and OMTKY3-psi[COO]-Leu18I in complex with Streptomyces griseus proteinase B (SGPB) and the structure of the free inhibitor, OMTKY-3-psi[CH2NH2+]-Asp19I
J. Mol. Biol.
305
839-849
2001
Streptomyces griseus
Manually annotated by BRENDA team
Joe, K.; Borgford, T.J.; Bennet, A.J.
Generation of a thermostable and denaturant-resistant peptide ligase
Biochemistry
43
7672-7677
2004
Streptomyces griseus
Manually annotated by BRENDA team
Jaswal, S.S.; Truhlar, S.M.; Dill, K.A.; Agard, D.A.
Comprehensive analysis of protein folding activation thermodynamics reveals a universal behavior violated by kinetically stable proteases
J. Mol. Biol.
347
355-366
2005
Streptomyces griseus
Manually annotated by BRENDA team
Truhlar, S.M.E.; Cunningham, E.L.; Agard, D.A.
The folding landscape of Streptomyces griseus protease B reveals the energetic costs and benefits associated with evolving kinetic stability
Protein Sci.
13
381-390
2004
Streptomyces griseus
Manually annotated by BRENDA team
Lee, T.W.; Qasim, M.A.; Laskowski, M.; James, M.N.
Structural insights into the non-additivity effects in the sequence-to-reactivity algorithm for serine peptidases and their inhibitors
J. Mol. Biol.
367
527-546
2007
Streptomyces griseus
Manually annotated by BRENDA team
Qasim, M.A.; Song, J.; Markley, J.L.; Laskowski, M.
Cleavage of peptide bonds bearing ionizable amino acids at P(1) by serine proteases with hydrophobic S(1) pocket
Biochem. Biophys. Res. Commun.
400
507-510
2010
Streptomyces griseus
Manually annotated by BRENDA team
Hemmi, H.; Kumazaki, T.; Kojima, S.; Yoshida, T.; Ohkubo, T.; Yokosawa, H.; Miura, K.; Kobayashi, Y.
Increasing the hydrolysis constant of the reactive site upon introduction of an engineered Cys14-Cys39 bond into the ovomucoid third domain from silver pheasant
J. Pept. Sci.
17
595-600
2011
Streptomyces griseus
Manually annotated by BRENDA team
Qasim, M.A.; Wang, L.; Qasim, S.; Lu, S.; Lu, W.; Wynn, R.; Yi, Z.P.; Laskowski, M.
Additivity-based design of the strongest possible turkey ovomucoid third domain inhibitors for porcine pancreatic elastase (PPE) and Streptomyces griseus protease B (SGPB)
FEBS Lett.
587
3021-3026
2013
Streptomyces griseus, Streptomyces griseus (P00777)
Manually annotated by BRENDA team