EzCatDB: D00219

DB codeD00219
RLCP classification1.13.30000.9
CATH domainDomain 13.30.70.80
Domain 23.40.50.200Catalytic domain
E.C.3.4.21.62
CSA1sca

CATH domainRelated DB codes (homologues)
3.40.50.200S00295,S00296,S00519

Enzyme Name
Swiss-protKEGG

P00780P00782P04189P07518
Protein nameSubtilisin CarlsbergSubtilisin BPN''Subtilisin ESubtilisinsubtilisin
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
SynonymsEC 3.4.21.62
EC 3.4.21.62
Subtilisin Novo
Subtilisin DFE
Alkaline protease
EC 3.4.21.62
EC 3.4.21.62
Alkaline mesentericopeptidase


Swiss-prot:Accession NumberP00780P00782P04189P07518
Entry nameSUBT_BACLISUBT_BACAMSUBT_BACSUSUBT_BACPU
ActivityHydrolysis of proteins with broad specificity for peptide bonds, and a preference for a large uncharged residue in P1. Hydrolyzes peptide amides.Hydrolysis of proteins with broad specificity for peptide bonds, and a preference for a large uncharged residue in P1. Hydrolyzes peptide amides.Hydrolysis of proteins with broad specificity for peptide bonds, and a preference for a large uncharged residue in P1. Hydrolyzes peptide amides.Hydrolysis of proteins with broad specificity for peptide bonds, and a preference for a large uncharged residue in P1. Hydrolyzes peptide amides.
Subunit
Monomer.

Subcellular locationSecreted.Secreted.Secreted.Secreted.
CofactorBinds 2 calcium ions per subunit.Binds 2 calcium ions per subunit.Binds 2 calcium ions per subunit.Binds 2 calcium ions per subunit.


CofactorsSubstratesProductsintermediates
KEGG-idC00076C00012C00017C00001C00012C00017I00087I00085I00086
CompoundCalciumPeptideProteinH2OPeptideProteinPeptidyl-tetrahedral intermediateAcyl-enzymeTetrahedral intermediate
Typedivalent metal (Ca2+, Mg2+)peptide/proteinpeptide/proteinH2Opeptide/proteinpeptide/protein


1scjBUnboundUnboundUnbound
UnboundUnboundUnboundUnboundUnbound
1spbPUnboundUnboundUnbound
UnboundUnboundUnboundUnboundUnbound
1af4ABound:_CAUnboundUnbound
UnboundUnboundUnboundUnboundUnbound
1a2qABound:2x_CAUnboundUnbound
UnboundUnboundUnboundUnboundUnbound
1ak9ABound:2x_CAUnboundUnbound
UnboundUnboundUnboundUnboundUnbound
1aqnABound:2x_CAUnboundUnbound
UnboundUnboundUnboundUnboundUnbound
1au9ABound:2x_CAUnboundUnbound
UnboundUnboundUnboundUnboundUnbound
1av7AAnalogue:2x_NAUnboundUnbound
UnboundUnboundUnboundUnboundUnbound
1avtAAnalogue:2x_NAUnboundUnbound
UnboundUnboundUnboundUnboundUnbound
1be6ABound:_CAUnboundUnbound
UnboundUnboundUnboundIntermediate-analogue:TCAUnbound
1be8ABound:_CAUnboundUnbound
UnboundUnboundUnboundIntermediate-analogue:TCAUnbound
1bfkABound:_CAUnboundUnbound
UnboundUnboundUnboundUnboundUnbound
1bfuABound:_CAUnboundUnbound
UnboundUnboundUnboundUnboundUnbound
1c3lABound:2x_CAUnboundUnbound
Analogue:FMT 285UnboundUnboundUnboundUnbound
1cseEBound:2x_CAUnboundBound:LEU 45-ASP 46(chain I)
UnboundUnboundUnboundUnboundUnbound
1duiAAnalogue:_NAUnboundUnbound
UnboundUnboundUnboundUnboundTransition-state-analogue:DFP
1gnvAUnboundUnboundUnbound
UnboundUnboundUnboundUnboundUnbound
1lw6EBound:_CAUnboundBound:MET 59-GLU 60(chain I)
UnboundUnboundUnboundUnboundUnbound
1meeABound:2x_CAUnboundBound:LYS 45-ASP 46(chain I)
UnboundUnboundUnboundUnboundUnbound
1oyvABound:_CAUnboundBound:PHE 62-ASN 63(chain I)
UnboundUnboundUnboundUnboundUnbound
1oyvBBound:_CAUnboundBound:ARG 5-GLU 6(chain I)
UnboundUnboundUnboundUnboundUnbound
1s01ABound:_CAUnboundUnbound
UnboundUnboundUnboundUnboundUnbound
1s02ABound:_CAUnboundUnbound
UnboundUnboundUnboundUnboundUnbound
1sbcABound:_CAUnboundUnbound
UnboundUnboundUnboundUnboundUnbound
1sbhABound:2x_CAUnboundUnbound
UnboundUnboundUnboundUnboundUnbound
1sbiABound:_CAUnboundUnbound
UnboundUnboundUnboundUnboundUnbound
1sbnEBound:2x_CAUnboundBound:ARG 45-ASP 46(chain I)
UnboundUnboundUnboundUnboundUnbound
1sbtAUnboundUnboundUnbound
UnboundUnboundUnboundUnboundUnbound
1scaABound:2x_CAUnboundUnbound
UnboundUnboundUnboundUnboundUnbound
1scbABound:_CAUnboundUnbound
UnboundUnboundUnboundUnboundUnbound
1scdABound:2x_CAUnboundUnbound
UnboundUnboundUnboundUnboundUnbound
1scnEBound:2x_CAUnboundUnbound
UnboundUnboundUnboundIntermediate-bound:BOC-ALA-PRO-APE(chain I)Unbound
1scjABound:2x_CAUnboundUnbound
UnboundBound:TYR 377(chain B)UnboundUnboundUnbound
1selABound:2x_CAUnboundUnbound
UnboundUnboundUnboundUnboundUnbound
1selBBound:2x_CAUnboundUnbound
UnboundUnboundUnboundUnboundUnbound
1sibEBound:2x_CAUnboundBound:LEU 45-ASP 46(chain I)
UnboundUnboundUnboundUnboundUnbound
1spbSAnalogue:_NAUnboundUnbound
UnboundBound:TYR 77(chain P)UnboundUnboundUnbound
1st2ABound:2x_CAUnboundUnbound
UnboundUnboundUnboundUnboundUnbound
1suaAUnboundUnboundUnbound
Bound:ALA-LEU-ALA-LEU(chain C)UnboundUnboundUnboundUnbound
1subABound:_CAUnboundUnbound
UnboundUnboundUnboundUnboundUnbound
1sucAAnalogue:__KUnboundUnbound
UnboundUnboundUnboundUnboundUnbound
1sudABound:2x_CAUnboundUnbound
UnboundUnboundUnboundUnboundUnbound
1sueAAnalogue:_NAUnboundUnbound
UnboundUnboundUnboundUnboundTransition-state-analogue:DFP
1supABound:_CAUnboundUnbound
UnboundUnboundUnboundUnboundTransition-state-analogue:PMS
1ubnABound:2x_CAUnboundUnbound
UnboundUnboundUnboundUnboundUnbound
1vsbAUnboundUnboundUnbound
UnboundUnboundUnboundUnboundUnbound
1yjaABound:2x_CAUnboundUnbound
UnboundUnboundUnboundUnboundUnbound
1yjbABound:2x_CAUnboundUnbound
UnboundUnboundUnboundUnboundUnbound
1yjcABound:2x_CAUnboundUnbound
UnboundUnboundUnboundUnboundUnbound
2sbtAUnboundUnboundUnbound
UnboundUnboundUnboundUnboundUnbound
2secEBound:3x_CAUnboundBound:LEU 59-ASP 60(chain I)
UnboundUnboundUnboundUnboundUnbound
2sicEBound:2x_CAUnboundBound:MET 73-VAL 74(chain I)
UnboundUnboundUnboundUnboundUnbound
2sniEBound:2x_CAUnboundBound:MET 59-GLU 60(chain I)
UnboundUnboundUnboundUnboundUnbound
2st1ABound:2x_CAUnboundUnbound
UnboundUnboundUnboundUnboundUnbound
3sicEBound:2x_CAUnboundBound:LYS 73-VAL 74(chain I)
UnboundUnboundUnboundUnboundUnbound
3vsbAAnalogue:2x_NAUnboundUnbound
UnboundUnboundUnboundUnboundUnbound
5sicEBound:2x_CAUnboundBound:LYS 73-VAL 74(chain I)
UnboundUnboundUnboundUnboundUnbound

Active-site residues
resource
Swiss-prot;P00780, P00782, P04189, P07518
pdbCatalytic residuesModified residuesMain-chain involved in catalysiscomment
1scjB



1spbP



1af4AASP 32;HIS 64;ASN 155;THR 220;SER 221

SER 221

1a2qAASP 32;HIS 64;ASN 155;THR 220;       
MIS 221
MIS 221
mutant T22C, S87C, G169A, N218S
1ak9AASP 32;HIS 64;ASN 155;THR 220;SER 221

SER 221
mutant T22C, M50F, S87C, G169A, Y217K, N218S
1aqnAASP 32;HIS 64;ASN 155;THR 220;SER 221

SER 221
mutant T22C, M50F, S87C, G169A, Q206C, Y217K, N218S
1au9AASP 32;HIS 64;ASN 155;THR 220;SER 221

SER 221
mutant T22C, M50F, S87C, G169A, Q206C, Y217K, N218S
1av7AASP 32;HIS 64;ASN 155;THR 220;       
SBL 221
SBL 221

1avtAASP 32;HIS 64;ASN 155;THR 220;       
CLD 221
CLD 221

1be6AASP 32;HIS 64;ASN 155;THR 220;SER 221

SER 221

1be8AASP 32;HIS 64;ASN 155;THR 220;SER 221

SER 221

1bfkAASP 32;HIS 64;ASN 155;THR 220;SER 221

SER 221

1bfuAASP 32;HIS 64;ASN 155;THR 220;SER 221

SER 221

1c3lAASP 32;HIS 64;ASN 155;THR 220;SER 221

SER 221

1cseEASP 32;HIS 64;ASN 155;THR 220;SER 221

SER 221

1duiAASP 32;HIS 64;ASN 155;THR 220;SER 221

SER 221

1gnvAASP 32;HIS 64;ASN 155;THR 220;       
MIS 221
MIS 221

1lw6EASP 32;HIS 64;ASN 155;THR 220;SER 221

SER 221

1meeAASP 32;HIS 64;ASN 155;THR 220;SER 221

SER 221

1oyvAASP 32;HIS 64;ASN 155;THR 220;SER 221

SER 221

1oyvBASP 32;HIS 64;ASN 155;THR 220;SER 221

SER 221

1s01AASP 32;HIS 64;ASN 155;THR 220;SER 221

SER 221
mutant M50F, N76D, G169A, Q206C, Y217K, N218S
1s02AASP 32;HIS 64;ASN 155;THR 220;SER 221

SER 221
mutant Q19E, Q271E
1sbcAASP 32;HIS 64;ASN 155;THR 220;SER 221

SER 221

1sbhAASP 32;HIS 64;ASN 155;THR 220;SER 221

SER 221
mutant M50F, N76D, G169A, Q206C, N218S, K256Y
1sbiAASP 32;HIS 64;ASN 155;THR 220;SER 221

SER 221
mutant M50F, N76D, G169A, Q206C, N218S
1sbnEASP 32;HIS 64;ASN 155;THR 220;SER 221

SER 221

1sbtAASP 32;HIS 64;ASN 155;THR 220;SER 221

SER 221

1scaAASP 32;HIS 64;ASN 155;THR 220;SER 221

SER 221

1scbAASP 32;HIS 64;ASN 155;THR 220;SER 221

SER 221

1scdAASP 32;HIS 64;ASN 155;THR 220;SER 221

SER 221

1scnEASP 32;HIS 64;ASN 155;THR 220;SER 221

SER 221

1scjAASP 32;HIS 64;ASN 155;THR 220;       

       
mutant S221C
1selAASP 32;HIS 64;ASN 155;THR 220;       
SEC 221
SEC 221

1selBASP 32;HIS 64;ASN 155;THR 220;       
SEC 221
SEC 221

1sibEASP 32;HIS 64;ASN 155;THR 220;SER 221

SER 221

1spbS      ;HIS 64;ASN 155;THR 220;       

       
mutant D32N, K43N, M50F, A73L, Q206V, Y217K, N218S, S221A, deletion 75-83
1st2AASP 32;HIS 64;ASN 155;THR 220;SER 221

SER 221

1suaAASP 32;HIS 64;ASN 155;THR 220;       

       
mutant K43N, M50F, G73L, Q206V, Y217K, N218S, S221A, Q271E, deletion 75-83
1subAASP 32;HIS 64;ASN 155;THR 220;       

       
mutant N218S, S221C
1sucAASP 32;HIS 64;ASN 155;THR 220;       

       
mutant M50P, Y217K, N218N, S221C, deletion 75-83
1sudAASP 32;HIS 64;ASN 155;THR 220;       

       
mutant M50P, Y217K, N218S, S221C
1sueAASP 32;HIS 64;ASN 155;THR 220;SER 221

SER 221
mutant Q2K, S3C, P5S, K43N, M50F, A73L, Q206C, Y217K, N218S, deletion 75-83
1supAASP 32;HIS 64;ASN 155;THR 220;SER 221

SER 221

1ubnAASP 32;HIS 64;ASN 155;THR 220;       
SOC 221
SOC 221

1vsbAASP 32;HIS 64;ASN 155;THR 220;       
CLB 221
CLB 221

1yjaAASP 32;HIS 64;ASN 155;THR 220;SER 221

SER 221
mutant M50F, N76D, G169A, Q206C, N218S, K256Y
1yjbAASP 32;HIS 64;ASN 155;THR 220;SER 221

SER 221
mutant M50F, N76D, G169A, Q206C, N218S, K256Y
1yjcAASP 32;HIS 64;ASN 155;THR 220;SER 221

SER 221
mutant M50F, N76D, G169A, Q206C, N218S, K256Y
2sbtAASP 32;HIS 64;ASN 155;THR 220;SER 221

SER 221

2secEASP 32;HIS 64;ASN 155;THR 220;SER 221

SER 221

2sicEASP 32;HIS 64;ASN 155;THR 220;SER 221

SER 221

2sniEASP 32;HIS 64;ASN 155;THR 220;SER 221

SER 221

2st1AASP 32;HIS 64;ASN 155;THR 220;SER 221

SER 221

3sicEASP 32;HIS 64;ASN 155;THR 220;SER 221

SER 221

3vsbAASP 32;HIS 64;ASN 155;THR 220;       
SBD 221
SBD 221

5sicEASP 32;HIS 64;ASN 155;THR 220;SER 221

SER 221


References for Catalytic Mechanism
ReferencesSectionsNo. of steps in catalysis
[2]

[5]

[8]p.397-399
[9]Fig.1
[10]p.6595
[11]p.7906
[12]p.275
[16]p.723
[17]Fig.1
[18]p.1219-1220
[19]Fig.1, p.11800
[20]Fig.2
[22]p.314-316
[25]Fig.4
[55]Fig.5

references
[1]
CommentsACTIVE SITE.
Medline ID69104413
PubMed ID5249818
JournalProc Natl Acad Sci U S A
Year1968
Volume61
Pages1440-7
AuthorsMarkland FS, Shaw E, Smith EL
TitleIdentification of histidine 64 in the active site of subtilisin.
Related Swiss-protP00782
[2]
CommentsX-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).
Medline ID72035041
PubMed ID4399039
JournalPhilos Trans R Soc Lond B Biol Sci
Year1970
Volume257
Pages119-24
AuthorsAlden RA, Wright CS, Kraut J
TitleA hydrogen-bond network at the active site of subtilisin BPN'.
Related Swiss-protP00782
[3]
CommentsX-ray crystallography
PubMed ID5160720
JournalBiochem Biophys Res Commun
Year1971
Volume45
Pages337-44
AuthorsAlden RA, Birktoft JJ, Kraut J, Robertus JD, Wright CS
TitleAtomic coordinates for subtilisin BPN' (or Novo).
Related PDB1sbt
[4]
CommentsX-ray crystallography
PubMed ID4508127
JournalCold Spring Harb Symp Quant Biol
Year1972
Volume36
Pages107-16
AuthorsDrenth J, Hol WG, Jansonius JN, Koekoek R
TitleA comparison of the three-dimensional structures of subtilisin BPN' and subtilisin novo.
Related PDB2sbt
[5]
CommentsX-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF COMPLEX WITH INHIBITOR.
Medline ID85033707
PubMed ID6387152
JournalJ Mol Biol
Year1984
Volume178
Pages389-414
AuthorsHirono S, Akagawa H, Mitsui Y, Iitaka Y
TitleCrystal structure at 2.6 A resolution of the complex of subtilisin BPN' with streptomyces subtilisin inhibitor.
Related Swiss-protP00782
[6]
PubMed ID3519213
JournalEMBO J
Year1986
Volume5
Pages813-8
AuthorsBode W, Papamokos E, Musil D, Seemueller U, Fritz H
TitleRefined 1.2 A crystal structure of the complex formed between subtilisin Carlsberg and the inhibitor eglin c. Molecular structure of eglin and its detailed interaction with subtilisin.
[7]
CommentsX-ray crystallography
PubMed ID3301348
JournalEur J Biochem
Year1987
Volume166
Pages673-92
AuthorsBode W, Papamokos E, Musil D
TitleThe high-resolution X-ray crystal structure of the complex formed between subtilisin Carlsberg and eglin c, an elastase inhibitor from the leech Hirudo medicinalis. Structural analysis, subtilisin structure and interface geometry.
Related PDB1cse
[8]
PubMed ID3299704
JournalScience
Year1987
Volume237
Pages394-9
AuthorsCarter P, Wells JA
TitleEngineering enzyme specificity by "substrate-assisted catalysis".
[9]
PubMed ID3282170
JournalNature
Year1988
Volume332
Pages564-8
AuthorsCarter P, Wells JA
TitleDissecting the catalytic triad of a serine protease.
[10]
CommentsX-ray crystallography
PubMed ID3064813
JournalBiochemistry
Year1988
Volume27
Pages6582-98
AuthorsMcPhalen CA, James MN
TitleStructural comparison of two serine proteinase-protein inhibitor complexes: eglin-c-subtilisin Carlsberg and CI-2-subtilisin Novo.
Related PDB2sec,2sni
[11]
CommentsX-ray crystallography
PubMed ID3286644
JournalJ Biol Chem
Year1988
Volume263
Pages7895-906
AuthorsBott R, Ultsch M, Kossiakoff A, Graycar T, Katz B, Power S
TitleThe three-dimensional structure of Bacillus amyloliquefaciens subtilisin at 1.8 A and an analysis of the structural consequences of peroxide inactivation.
Related PDB1st2,2st1
[12]
CommentsX-ray crystallography
PubMed ID3150541
JournalProtein Eng
Year1988
Volume2
Pages271-6
AuthorsNeidhart DJ, Petsko GA
TitleThe refined crystal structure of subtilisin Carlsberg at 2.5 A resolution.
Related PDB1sbc
[13]
CommentsX-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF MUTANT.
Medline ID90057412
PubMed ID2684274
JournalBiochemistry
Year1989
Volume28
Pages7205-13
AuthorsPantoliano MW, Whitlow M, Wood JF, Dodd SW, Hardman KD, Rollence ML, Bryan PN
TitleLarge increases in general stability for subtilisin BPN' through incremental changes in the free energy of unfolding.
Related PDB1s01,1a2q,1ak9,1au9
Related Swiss-protP00782
[14]
CommentsX-ray crystallography
PubMed ID2127106
JournalProtein Eng
Year1990
Volume4
Pages87-97
AuthorsErwin CR, Barnett BL, Oliver JD, Sullivan JF
TitleEffects of engineered salt bridges on the stability of subtilisin BPN'.
Related PDB1s02
[15]
PubMed ID2199972
JournalProteins
Year1990
Volume7
Pages343-57
AuthorsKatz B, Kossiakoff AA
TitleCrystal structures of subtilisin BPN' variants containing disulfide bonds and cavities: concerted structural rearrangements induced by mutagenesis.
[16]
CommentsX-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
Medline ID92172311
PubMed ID1793542
JournalActa Crystallogr B
Year1991
Volume47
Pages707-30
AuthorsDauter Z, Betzel C, Genov N, Pipon N, Wilson KS
TitleComplex between the subtilisin from a mesophilic bacterium and the leech inhibitor eglin-C.
Related PDB1mee
Related Swiss-protP07518
[17]
PubMed ID2059622
JournalBiochemistry
Year1991
Volume30
Pages6142-8
AuthorsCarter P, Abrahmsen L, Wells JA
TitleProbing the mechanism and improving the rate of substrate-assisted catalysis in subtilisin BPN'.
[18]
PubMed ID1991100
JournalBiochemistry
Year1991
Volume30
Pages1211-21
AuthorsKossiakoff AA, Ultsch M, White S, Eigenbrot C
TitleNeutron structure of subtilisin BPN': effects of chemical environment on hydrogen-bonding geometries and the pattern of hydrogen-deuterium exchange in secondary structure elements.
[19]
PubMed ID1904870
JournalJ Biol Chem
Year1991
Volume266
Pages11797-800
AuthorsBraxton S, Wells JA
TitleThe importance of a distal hydrogen bonding group in stabilizing the transition state in subtilisin BPN'.
[20]
PubMed ID1904871
JournalJ Biol Chem
Year1991
Volume266
Pages11801-9
AuthorsMizushima N, Spellmeyer D, Hirono S, Pearlman D, Kollman P
TitleFree energy perturbation calculations on binding and catalysis after mutating threonine 220 in subtilisin.
[21]
CommentsX-ray crystallography
PubMed ID1992167
JournalJ Mol Biol
Year1991
Volume217
Pages353-71
AuthorsHeinz DW, Priestle JP, Rahuel J, Wilson KS, Grutter MG
TitleRefined crystal structures of subtilisin novo in complex with wild-type and two mutant eglins. Comparison with other serine proteinase inhibitor complexes.
Related PDB1sbn,1sib
[22]
CommentsX-ray crystallography
PubMed ID1920411
JournalJ Mol Biol
Year1991
Volume221
Pages309-25
AuthorsTakeuchi Y, Satow Y, Nakamura KT, Mitsui Y
TitleRefined crystal structure of the complex of subtilisin BPN' and Streptomyces subtilisin inhibitor at 1.8 A resolution.
Related PDB2sic
[23]
CommentsX-ray crystallography
PubMed ID1891457
JournalProtein Eng
Year1991
Volume4
Pages501-8
AuthorsTakeuchi Y, Noguchi S, Satow Y, Kojima S, Kumagai I, Miura K, Nakamura KT, Mitsui Y
TitleMolecular recognition at the active site of subtilisin BPN': crystallographic studies using genetically engineered proteinaceous inhibitor SSI (Streptomyces subtilisin inhibitor).
Related PDB3sic,5sic
[24]
PubMed ID1453465
JournalJ Mol Biol
Year1992
Volume228
Pages580-95
AuthorsGoddette DW, Paech C, Yang SS, Mielenz JR, Bystroff C, Wilke ME, Fletterick RJ
TitleThe crystal structure of the Bacillus lentus alkaline protease, subtilisin BL, at 1.4 A resolution.
[25]
PubMed ID8268166
JournalBiochemistry
Year1993
Volume32
Pages13909-16
AuthorsJackson SE, Fersht AR
TitleContribution of long-range electrostatic interactions to the stabilization of the catalytic transition state of the serine protease subtilisin BPN'.
[26]
PubMed ID8347611
JournalBiochemistry
Year1993
Volume32
Pages8112-9
AuthorsStrausberg S, Alexander P, Wang L, Schwarz F, Bryan P
TitleCatalysis of a protein folding reaction: thermodynamic and kinetic analysis of subtilisin BPN' interactions with its propeptide fragment.
[27]
CommentsX-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF MUTANT WITH SELENOCYSTEINE-325.
Medline ID93291170
PubMed ID8512925
JournalBiochemistry
Year1993
Volume32
Pages6157-64
AuthorsSyed R, Wu ZP, Hogle JM, Hilvert D
TitleCrystal structure of selenosubtilisin at 2.0-A resolution.
Related PDB1sel
Related Swiss-protP00780
[28]
CommentsX-ray crystallography
PubMed ID8378343
JournalProc Natl Acad Sci U S A
Year1993
Volume90
Pages8653-7
AuthorsFitzpatrick PA, Steinmetz AC, Ringe D, Klibanov AM
TitleEnzyme crystal structure in a neat organic solvent.
Related PDB1sca,1scb
[29]
PubMed ID8332597
JournalProtein Eng
Year1993
Volume6
Pages397-408
AuthorsHeiner AP, Berendsen HJ, van Gunsteren WF
TitleStructure prediction of subtilisin BPN' mutants using molecular dynamics methods.
[30]
CommentsX-ray crystallography
PubMed ID8332608
JournalProteins
Year1993
Volume16
Pages205-13
AuthorsGallagher T, Bryan P, Gilliland GL
TitleCalcium-independent subtilisin by design.
Related PDB1sub,1suc,1sud
[31]
CommentsX-ray crystallography
PubMed ID8297378
JournalBiochem Biophys Res Commun
Year1994
Volume198
Pages675-81
AuthorsFitzpatrick PA, Ringe D, Klibanov AM
TitleX-ray crystal structure of cross-linked subtilisin Carlsberg in water vs. acetonitrile.
Related PDB1scd
[32]
CommentsX-ray crystallography
PubMed ID8068694
JournalBiochemistry
Year1994
Volume33
Pages10535-44
AuthorsSteinmetz AC, Demuth HU, Ringe D
TitleInactivation of subtilisin Carlsberg by N-((tert-butoxycarbonyl)alanylprolylphenylalanyl)-O-benzoylhydroxyl- amine: formation of a covalent enzyme-inhibitor linkage in the form of a carbamate derivative.
Related PDB1scn
[33]
PubMed ID7547973
JournalBiochemistry
Year1995
Volume34
Pages12302-10
AuthorsWangikar PP, Rich JO, Clark DS, Dordick JS
TitleProbing enzymic transition state hydrophobicities.
[34]
CommentsX-ray crystallography
PubMed ID8535784
JournalStructure
Year1995
Volume3
Pages907-14
AuthorsGallagher T, Gilliland G, Wang L, Bryan P
TitleThe prosegment-subtilisin BPN' complex: crystal structure of a specific 'foldase'.
Related PDB1spb
[35]
CommentsX-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS)
JournalActa Crystallogr D Biol Crystallogr
Year1996
Volume52
Pages1125-35
AuthorsGallagher T, Oliver J, Bott R, Betzel C, Gilliland GL
TitleSubtilisin BPN' at 1.6-A resolution: analysis for discrete disorder and comparison of crystal forms.
Related Swiss-protP00782
[36]
PubMed ID8796321
JournalAdv Exp Med Biol
Year1996
Volume379
Pages159-69
AuthorsGilliland GL, Gallagher DT, Alexander P, Bryan P
TitleCrystal structure analysis of subtilisin BPN' mutants engineered for studying thermal stability.
[37]
PubMed ID8796307
JournalAdv Exp Med Biol
Year1996
Volume379
Pages21-7
AuthorsNonaka T, Suzuki T, Tanaka N, Saito S, Senda T, Miura K, Mitsui Y
TitleStructure and function of subtilisin BPN' as studied through crystallographic studies on a series of its complexes with genetically engineered proteinaceous inhibitor SSI.
[38]
CommentsX-ray crystallography
JournalJ Am Chem Soc
Year1996
Volume118
Pages1645-50
AuthorsKidd RD, Yennawar HP, Sears P, Wong CH, Farber GK
TitleA Weak Calcium Binding Site in Subtilisin BPN' Has a Dramatic Effect on Protein Stability.
Related PDB1sbi
[39]
CommentsX-ray crystallography
PubMed ID9113975
JournalProc Natl Acad Sci U S A
Year1997
Volume94
Pages4250-5
AuthorsSchmitke JL, Stern LJ, Klibanov AM
TitleThe crystal structure of subtilisin Carlsberg in anhydrous dioxane and its comparison with those in water and acetonitrile.
Related PDB1af4
[40]
CommentsX-ray crystallography
PubMed ID9675126
JournalBiochem Biophys Res Commun
Year1998
Volume248
Pages273-7
AuthorsSchmitke JL, Stern LJ, Klibanov AM
TitleOrganic solvent binding to crystalline subtilisin1 in mostly aqueous media and in the neat solvents.
Related PDB1bfk,1bfu
[41]
CommentsX-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 106-379.
Medline ID98087517
PubMed ID9425066
JournalBiochemistry
Year1998
Volume37
Pages451-62
AuthorsStoll VS, Eger BT, Hynes RC, Martichonok V, Jones JB, Pai EF
TitleDifferences in binding modes of enantiomers of 1-acetamido boronic acid based protease inhibitors: crystal structures of gamma-chymotrypsin and subtilisin Carlsberg complexes.
Related PDB1av7,1avt,1vsb
Related Swiss-protP00780
[42]
CommentsX-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
Medline ID99030466
PubMed ID9811547
JournalJ Mol Biol
Year1998
Volume284
Pages137-44
AuthorsJain SC, Shinde U, Li Y, Inouye M, Berman HM
TitleThe crystal structure of an autoprocessed Ser221Cys-subtilisin E-propeptide complex at 2.0 A resolution.
Related PDB1scj
Related Swiss-protP04189
[43]
CommentsX-ray crystallography
JournalJournal of Crystal Growth
Year1998
Volume193
Pages665-73
AuthorsGallagher DT, Pan QW, Gilliland GL
TitleMechanism of ionic strength dependence of crystal growth rates in a subtilisin variant.
Related PDB1sue
[44]
CommentsX-ray crystallography
PubMed ID9789015
JournalProc Natl Acad Sci U S A
Year1998
Volume95
Pages12918-23
AuthorsSchmitke JL, Stern LJ, Klibanov AM
TitleComparison of x-ray crystal structures of an acyl-enzyme intermediate of subtilisin Carlsberg formed in anhydrous acetonitrile and in water.
Related PDB1be6,1be8
[45]
CommentsX-ray crystallography
PubMed ID9552156
JournalProteins
Year1998
Volume31
Pages21-32
AuthorsAlmog O, Gallagher T, Tordova M, Hoskins J, Bryan P, Gilliland GL
TitleCrystal structure of calcium-independent subtilisin BPN' with restored thermal stability folded without the prodomain.
Related PDB1sua
[46]
CommentsX-ray crystallography
PubMed ID9443341
JournalProteins
Year1998
Volume30
Pages61-73
AuthorsPrange T, Schiltz M, Pernot L, Colloc'h N, Longhi S, Bourguet W, Fourme R
TitleExploring hydrophobic sites in proteins with xenon or krypton.
Related PDB1c3l
[47]
CommentsX-ray crystallography
PubMed ID10350485
JournalBiochemistry
Year1999
Volume38
Pages6659-67
AuthorsDinakarpandian D, Shenoy BC, Hilvert D, McRee DE, McTigue M, Carey PR
TitleElectric fields in active sites: substrate switching from null to strong fields in thiol- and selenol-subtilisins.
Related PDB1ubn
[48]
CommentsX-ray crystallography
PubMed ID10048334
JournalProtein Sci
Year1999
Volume8
Pages410-7
AuthorsKidd RD, Sears P, Huang DH, Witte K, Wong CH, Farber GK
TitleBreaking the low barrier hydrogen bond in a serine protease.
Related PDB1yja,1yjb,1yjc
[49]
PubMed ID11524007
JournalBiochemistry
Year2001
Volume40
Pages10634-9
AuthorsAlexander PA, Ruan B, Bryan PN
TitleCation-dependent stability of subtilisin.
[50]
PubMed ID11524008
JournalBiochemistry
Year2001
Volume40
Pages10640-4
AuthorsAlexander PA, Ruan B, Strausberg SL, Bryan PN
TitleStabilizing mutations and calcium-dependent stability of subtilisin.
[51]
PubMed ID11523982
JournalBiochemistry
Year2001
Volume40
Pages10411-6
AuthorsStratton JR, Pelton JG, Kirsch JF
TitleA novel engineered subtilisin BPN' lacking a low-barrier hydrogen bond in the catalytic triad.
[52]
CommentsX-ray crystallography
PubMed ID12011071
JournalJ Biol Chem
Year2002
Volume277
Pages27553-8
AuthorsAlmog O, Gallagher DT, Ladner JE, Strausberg S, Alexander P, Bryan P, Gilliland GL
TitleStructural basis of thermostability. Analysis of stabilizing mutations in subtilisin BPN'.
Related PDB1gnv
[53]
PubMed ID11925221
JournalJ Org Chem
Year2002
Volume67
Pages2144-51
AuthorsEma T, Jittani M, Furuie K, Utaka M, Sakai T
Title5-[4-(1-Hydroxyethyl)phenyl]-10,15,20-triphenylporphyrin as a probe of the transition-state conformation in hydrolase-catalyzed enantioselective transesterifications.
[54]
CommentsX-ray crystallography
PubMed ID12142461
JournalProc Natl Acad Sci U S A
Year2002
Volume99
Pages10316-21
AuthorsRadisky ES, Koshland DE Jr
TitleA clogged gutter mechanism for protease inhibitors.
Related PDB1lw6
[55]
CommentsX-ray crystallography
PubMed ID12684499
JournalJ Biol Chem
Year2003
Volume278
Pages24062-71
AuthorsBarrette-Ng IH, Ng KK, Cherney MM, Pearce G, Ryan CA, James MN
TitleStructural basis of inhibition revealed by a 1:2 complex of the two-headed tomato inhibitor-II and subtilisin Carlsberg.
Related PDB1oyv
[56]
PubMed ID12649438
JournalProtein Sci
Year2003
Volume12
Pages794-810
AuthorsDay RM, Thalhauser CJ, Sudmeier JL, Vincent MP, Torchilin EV, Sanford DG, Bachovchin CW, Bachovchin WW
TitleTautomerism, acid-base equilibria, and H-bonding of the six histidines in subtilisin BPN' by NMR.

comments
This enzyme belongs to the peptidase family-S8.
The calcium ions are not involved in catalysis.
This enzyme has got a classic catalytic triad, composed of Ser/His/Asp, as in trypsin (D00197 in EzCatDB), suggesting that it has a similar mechanism to that of trypsin. However, in contrast to trypsin-like enzymes (where mainchain amide groups form an oxyanion hole), sidechains of Asn155 and Thr220 form an oxyanion hole, which stabilizes the transition-state, together with the mainchain amide group of Ser221 (see [11], [19] & [20]).

createdupdated
2004-11-122011-02-21
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)

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