EzCatDB: D00224

DB codeD00224
RLCP classification1.13.30000.10
CATH domainDomain 12.40.10.10Catalytic domain
Domain 22.40.10.10Catalytic domain
E.C.3.4.21.81
CSA1ds2

CATH domainRelated DB codes (homologues)
2.40.10.10M00139,D00214,M00167,D00426,M00133,D00428,D00429,D00430,D00431,D00432,D00433,D00434,D00435,M00227,M00209,D00194,D00197,D00211,D00212,D00216,M00212,D00497,M00217,M00216,D00528,D00848,D00850,D00851,D00852,D00855,M00152,M00155,M00157,M00181,M00315,M00316,M00317,M00348,M00349,T00074,T00410,T00411

Enzyme Name
Swiss-protKEGG

P00777
Protein nameStreptogrisin-Bstreptogrisin B
Streptomyces griseus protease B
pronase B
serine proteinase B
Streptomyces griseus proteinase B
Streptomyces griseus proteinase 1
Streptomyces griseus serine proteinase B
SynonymsEC 3.4.21.81
Serine protease B
SGPB
Pronase enzyme B


Swiss-prot:Accession NumberP00777
Entry namePRTB_STRGR
ActivityHydrolysis of proteins with trypsin-like specificity.
SubunitMonomer.
Subcellular location
Cofactor


SubstratesProductsintermediates
KEGG-idC00017C00012C00001C00017C00012I00087I00085I00086
CompoundProteinPeptideH2OProteinPeptidePeptidyl-tetrahedral intermediateAcyl-enzymeTetrahedral intermediate
Typepeptide/proteinpeptide/proteinH2Opeptide/proteinpeptide/protein


1csoE01UnboundUnbound
UnboundUnboundUnboundUnboundUnbound
1ct0E01UnboundUnbound
UnboundUnboundUnboundUnboundUnbound
1ct2E01UnboundUnbound
UnboundUnboundUnboundUnboundUnbound
1ct4E01UnboundUnbound
UnboundUnboundUnboundUnboundUnbound
1ds2E01UnboundUnbound
UnboundUnboundUnboundUnboundUnbound
1sgdE01UnboundUnbound
UnboundUnboundUnboundUnboundUnbound
1sgeE01UnboundUnbound
UnboundUnboundUnboundUnboundUnbound
1sgnE01UnboundUnbound
UnboundUnboundUnboundUnboundUnbound
1sgpE01UnboundUnbound
UnboundUnboundUnboundUnboundUnbound
1sgqE01UnboundUnbound
UnboundUnboundUnboundUnboundUnbound
1sgrE01UnboundUnbound
UnboundUnboundUnboundUnboundUnbound
1sgyE01UnboundUnbound
UnboundUnboundUnboundUnboundUnbound
2sgdE01UnboundUnbound
UnboundUnboundUnboundUnboundUnbound
2sgeE01UnboundUnbound
UnboundUnboundUnboundUnboundUnbound
2sgfE01UnboundUnbound
UnboundUnboundUnboundUnboundUnbound
2sgpE01UnboundUnbound
UnboundUnboundUnboundUnboundUnbound
2sgqE01UnboundUnbound
UnboundUnboundUnboundUnboundUnbound
3sgbE01UnboundUnbound
UnboundUnboundUnboundUnboundUnbound
3sgqE01UnboundUnbound
UnboundUnboundUnboundUnboundUnbound
4sgbE01UnboundUnbound
UnboundUnboundUnboundUnboundUnbound
1csoE02UnboundAnalogue:ILE 18-GLU 19(chain I)
UnboundUnboundUnboundUnboundUnbound
1ct0E02UnboundAnalogue:SER 18-GLU 19(chain I)
UnboundUnboundUnboundUnboundUnbound
1ct2E02UnboundAnalogue:THR 18-GLU 19(chain I)
UnboundUnboundUnboundUnboundUnbound
1ct4E02UnboundAnalogue:VAL 18-GLU 19(chain I)
UnboundUnboundUnboundUnboundUnbound
1ds2E02UnboundAnalogue:1LU 18-GLU 19(chain I)
UnboundUnboundUnboundUnboundUnbound
1sgdE02UnboundAnalogue:ASP 18-GLU 19(chain I)
UnboundUnboundUnboundUnboundUnbound
1sgeE02UnboundAnalogue:GLU 18-GLU 19(chain I)
UnboundUnboundUnboundUnboundUnbound
1sgnE02UnboundAnalogue:ASN 18-GLU 19(chain I)
UnboundUnboundUnboundUnboundUnbound
1sgpE02UnboundAnalogue:ALA 18-GLU 19(chain I)
UnboundUnboundUnboundUnboundUnbound
1sgqE02UnboundAnalogue:GLY 18-GLU 19(chain I)
UnboundUnboundUnboundUnboundUnbound
1sgrE02UnboundAnalogue:LEU 18-GLU 19(chain I)
UnboundUnboundUnboundUnboundUnbound
1sgyE02UnboundAnalogue:TYR 18-GLU 19(chain I)
UnboundUnboundUnboundUnboundUnbound
2sgdE02UnboundAnalogue:ASP 18-GLU 19(chain I)
UnboundUnboundUnboundUnboundUnbound
2sgeE02UnboundAnalogue:GLU 18-GLU 19(chain I)
UnboundUnboundUnboundUnboundUnbound
2sgfE02UnboundAnalogue:PHE 18-GLU 19(chain I)
UnboundUnboundUnboundUnboundUnbound
2sgpE02UnboundAnalogue:PRO 18-GLU 19(chain I)
UnboundUnboundUnboundUnboundUnbound
2sgqE02UnboundAnalogue:GLN 18-GLU 19(chain I)
UnboundUnboundUnboundUnboundUnbound
3sgbE02UnboundAnalogue:LEU 18-GLU 19(chain I)
UnboundUnboundUnboundUnboundUnbound
3sgqE02UnboundAnalogue:GLN 18-GLU 19(chain I)
UnboundUnboundUnboundUnboundUnbound
4sgbE02UnboundAnalogue:LEU 38-ASN 39(chain I)
UnboundUnboundUnboundUnboundUnbound

Active-site residues
resource
PDB;1sgd, 1sge, 1sgn, 1sgp,1sgq,1sgr, 2sgd, 2sge, 2sgf, 2sgp, 2sgq, 3sgq & Swiss-prot;P00777 & literature [3], [5], [7]
pdbCatalytic residuesMain-chain involved in catalysis
1csoE01HIS 57;ASP 102

1ct0E01HIS 57;ASP 102

1ct2E01HIS 57;ASP 102

1ct4E01HIS 57;ASP 102

1ds2E01HIS 57;ASP 102

1sgdE01HIS 57;ASP 102

1sgeE01HIS 57;ASP 102

1sgnE01HIS 57;ASP 102

1sgpE01HIS 57;ASP 102

1sgqE01HIS 57;ASP 102

1sgrE01HIS 57;ASP 102

1sgyE01HIS 57;ASP 102

2sgdE01HIS 57;ASP 102

2sgeE01HIS 57;ASP 102

2sgfE01HIS 57;ASP 102

2sgpE01HIS 57;ASP 102

2sgqE01HIS 57;ASP 102

3sgbE01HIS 57;ASP 102

3sgqE01HIS 57;ASP 102

4sgbE01HIS 57;ASP 102

1csoE02SER 195
GLY 193;SER 195
1ct0E02SER 195
GLY 193;SER 195
1ct2E02SER 195
GLY 193;SER 195
1ct4E02SER 195
GLY 193;SER 195
1ds2E02SER 195
GLY 193;SER 195
1sgdE02SER 195
GLY 193;SER 195
1sgeE02SER 195
GLY 193;SER 195
1sgnE02SER 195
GLY 193;SER 195
1sgpE02SER 195
GLY 193;SER 195
1sgqE02SER 195
GLY 193;SER 195
1sgrE02SER 195
GLY 193;SER 195
1sgyE02SER 195
GLY 193;SER 195
2sgdE02SER 195
GLY 193;SER 195
2sgeE02SER 195
GLY 193;SER 195
2sgfE02SER 195
GLY 193;SER 195
2sgpE02SER 195
GLY 193;SER 195
2sgqE02SER 195
GLY 193;SER 195
3sgbE02SER 195
GLY 193;SER 195
3sgqE02SER 195
GLY 193;SER 195
4sgbE02SER 195
GLY 193;SER 195

References for Catalytic Mechanism
ReferencesSectionsNo. of steps in catalysis
[5]p.142
[7]p.431
[9]


references
[1]
CommentsACTIVE SITE.
Medline ID68124983
PubMed ID5636372
JournalBiochim Biophys Acta
Year1968
Volume151
Pages402-8
AuthorsWahlby S, Engstrom L
TitleStudies on Streptomyces griseus protease. II. The amino acid sequence around the reactive serine residue of DFP-sensitive components with esterase activity.
Related Swiss-protP00777
[2]
CommentsACTIVE SITE.
Medline ID74302902
PubMed ID4212092
JournalFEBS Lett
Year1974
Volume43
Pages81-5
AuthorsGertler A
TitleInhibition of Streptomyces griseus protease B by peptide chloromethyl ketones: partial mapping of the binding site and identification of the reactive residue.
Related Swiss-protP00777
[3]
CommentsX-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS), AND REVISIONS.
Medline ID76051298
PubMed ID1186854
JournalNature
Year1975
Volume257
Pages758-63
AuthorsDelbaere LT, Hutcheon WL, James MN, Thiessen WE
TitleTertiary structural differences between microbial serine proteases and pancreatic serine enzymes.
Related Swiss-protP00777
[4]
PubMed ID413567
JournalBiochemistry
Year1978
Volume17
Pages375-80
AuthorsBauer CA
TitleActive centers of Streptomyces griseus protease 1, Streptomyces griseus protease 3, and alpha-chymotrypsin: enzyme-substrate interactions.
[5]
CommentsX-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS), AND REVISIONS.
Medline ID79210651
PubMed ID110426
JournalCan J Biochem
Year1979
Volume57
Pages135-44
AuthorsDelbaere LT, Brayer GD, James MN
TitleThe 2.8 A resolution structure of Streptomyces griseus protease B and its homology with alpha-chymotrypsin and Streptomyces griseus protease A.
Related Swiss-protP00777
[6]
PubMed ID6769571
JournalCan J Biochem
Year1980
Volume58
Pages252-71
AuthorsJames MN
TitleAn X-ray crystallographic approach to enzyme structure and function.
[7]
PubMed ID6777499
JournalJ Mol Biol
Year1980
Volume139
Pages423-38
AuthorsJames MN, Brayer GD, Delbaere LT, Sielecki AR, Gertler A
TitleCrystal structure studies and inhibition kinetics of tripeptide chloromethyl ketone inhibitors with Streptomyces griseus protease B.
[8]
CommentsX-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF THIRD DOMAIN.
Medline ID83014993
PubMed ID6750612
JournalProc Natl Acad Sci U S A
Year1982
Volume79
Pages4868-72
AuthorsFujinaga M, Read RJ, Sielecki A, Ardelt W, Laskowski M Jr, James MN
TitleRefined crystal structure of the molecular complex of Streptomyces griseus protease B, a serine protease, with the third domain of the ovomucoid inhibitor from turkey.
[9]
CommentsX-ray crystallography
PubMed ID6414511
JournalBiochemistry
Year1983
Volume22
Pages4420-33
AuthorsRead RJ, Fujinaga M, Sielecki AR, James MN
TitleStructure of the complex of Streptomyces griseus protease B and the third domain of the turkey ovomucoid inhibitor at 1.8-A resolution.
Related PDB3sgb
[10]
CommentsX-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 55-106.
Medline ID89178636
PubMed ID2494344
JournalJ Mol Biol
Year1989
Volume205
Pages201-28
AuthorsGreenblatt HM, Ryan CA, James MN
TitleStructure of the complex of Streptomyces griseus proteinase B and polypeptide chymotrypsin inhibitor-1 from Russet Burbank potato tubers at 2.1 A resolution.
Related PDB4sgb
Related Swiss-protP00777
[11]
PubMed ID8495199
JournalProtein Sci
Year1993
Volume2
Pages786-99
AuthorsBigler TL, Lu W, Park SJ, Tashiro M, Wieczorek M, Wynn R, Laskowski M Jr
TitleBinding of amino acid side chains to preformed cavities: interaction of serine proteinases with turkey ovomucoid third domains with coded and noncoded P1 residues.
[12]
PubMed ID7499197
JournalJ Biol Chem
Year1995
Volume270
Pages27419-22
AuthorsAbul Qasim M, Ranjbar MR, Wynn R, Anderson S, Laskowski M Jr
TitleIonizable P1 residues in serine proteinase inhibitors undergo large pK shifts on complex formation.
[13]
CommentsX-ray crystallography
PubMed ID8535235
JournalProtein Sci
Year1995
Volume4
Pages1985-97
AuthorsHuang K, Lu W, Anderson S, Laskowski M Jr, James MN
TitleWater 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.
Related PDB1sgp,1sgq,1sgr
[14]
PubMed ID9020764
JournalBiochemistry
Year1997
Volume36
Pages673-9
AuthorsLu W, Qasim MA, Laskowski M Jr, Kent SB
TitleProbing intermolecular main chain hydrogen bonding in serine proteinase-protein inhibitor complexes: chemical synthesis of backbone-engineered turkey ovomucoid third domain.
[15]
PubMed ID9878379
JournalJ Mol Biol
Year1998
Volume284
Pages1683-94
AuthorsFujinaga M, Huang K, Bateman KS, James MN
TitleComputational analysis of the binding of P1 variants of domain 3 of turkey ovomucoid inhibitor to Streptomyces griseus protease B.
[16]
PubMed ID10712933
JournalChem Biol
Year2000
Volume7
Pages163-71
AuthorsElliott RJ, Bennet AJ, Braun CA, MacLeod AM, Borgford TJ
TitleActive-site variants of Streptomyces griseus protease B with peptide-ligation activity.
[17]
CommentsX-RAY DIFFRACTION
PubMed ID10739250
JournalProtein Sci
Year2000
Volume9
Pages83-94
AuthorsBateman KS, Anderson S, Lu W, Qasim MA, Laskowski M Jr, James MN
TitleDeleterious effects of beta-branched residues in the S1 specificity pocket of Streptomyces griseus proteinase B (SGPB): crystal structures of the turkey ovomucoid third domain variants Ile18I, Val18I, Thr18I, and Ser18I in complex with SGPB.
Related PDB1cso,1ct0,1ct2,1ct4
[18]
CommentsX-ray crystallography
PubMed ID11162096
JournalJ Mol Biol
Year2001
Volume305
Pages839-49
AuthorsBateman KS, Huang K, Anderson S, Lu W, Qasim MA, Laskowski M Jr, James MN
TitleContribution 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.
Related PDB1ds2,2sgp
[19]
PubMed ID14718653
JournalProtein Sci
Year2004
Volume13
Pages381-90
AuthorsTruhlar SM, Cunningham EL, Agard DA
TitleThe folding landscape of Streptomyces griseus protease B reveals the energetic costs and benefits associated with evolving kinetic stability.
[20]
PubMed ID15740746
JournalJ Mol Biol
Year2005
Volume347
Pages355-66
AuthorsJaswal SS, Truhlar SM, Dill KA, Agard DA
TitleComprehensive analysis of protein folding activation thermodynamics reveals a universal behavior violated by kinetically stable proteases.

comments
This enzyme belongs to the peptidase family-S1E.
This enzyme has got a catalytic triad composed of Ser/His/Asp, it should have the same mechanism as that of trypsin (D00197 in EzCatDB).

createdupdated
2003-10-142011-02-21


Copyright: Nozomi Nagano, JST & CBRC-AIST
Funded by PRESTO/Japan Science and Technology Corporation (JST) (December 2001 - November 2004)
Funded by Grant-in-Aid for Publication of Scientific Research Results/Japan Society for the Promotion of Science (JSPS) (April 2005 - March 2006)
Funded by Grant-in-Aid for Scientific Research (B)/Japan Society for the Promotion of Science (JSPS) (April 2005 - March 2008)
Funded by BIRD/Japan Science and Technology Corporation (JST) (September 2005 - September 2010)
Funded by BIRD/Japan Science and Technology Corporation (JST) (October 2007 - September 2010)
Funded by Grant-in-Aid for Publication of Scientific Research Results/Japan Society for the Promotion of Science (JSPS) (April 2011 - March 2012)

© Computational Biology Research Center, AIST, 2004 All Rights Reserved.