Information on EC 3.4.23.B9 - bovine leukemia virus protease

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The expected taxonomic range for this enzyme is: Bovine leukemia virus

EC NUMBER
COMMENTARY hide
3.4.23.B9
preliminary BRENDA-supplied EC number
RECOMMENDED NAME
GeneOntology No.
bovine leukemia virus protease
-
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
The best substrate YDPPAILPII is bearing the natural cleavage site between the matrix and the capsid proteins of BLV Gag precursor. polyprotein. Good cleavage of the peptide bonds: Leu-Pro, Leu-Val, Gly-Val and Leu-Pro
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of peptide bond
-
-
-
-
CAS REGISTRY NUMBER
COMMENTARY hide
144114-21-6
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
AELE-aminobutyric acid-LLSIPLA + H2O
AELE-aminobutyric acid-L + LSIPLA
show the reaction diagram
-
70% of the activity with YDPPAILPII
-
-
?
APQVLPVMHP + H2O
APQVL + PVMHP
show the reaction diagram
Gag polyprotein + H2O
?
show the reaction diagram
Gag-Pol polyprotein + H2O
?
show the reaction diagram
KAKVLVVQPK + H2O
KAKVL + VVQPK
show the reaction diagram
P4-substituted peptide
-
-
?
KDKVLVVQPK + H2O
KDKVL + VVQPK
show the reaction diagram
P4-substituted peptide
-
-
?
KGKVLVVQPK + H2O
KGKVL + VVQPK
show the reaction diagram
P4-substituted peptide
-
-
?
KGPPVILPIQAP + H2O
KGPPVIL + PIQAP
show the reaction diagram
-
-
-
?
KGPPVILPIQDP + H2O
KGPPVIL + PIQDP
show the reaction diagram
-
-
-
?
KLKVLVVQPK + H2O
KLKVL + VVQPK
show the reaction diagram
P4-substituted peptide
-
-
?
KPKVLVVQPK + H2O
KPKVL + VVQPK
show the reaction diagram
P4-substituted peptide
-
-
?
KQPAILVHTPG + H2O
KQPAIL + VHTPG
show the reaction diagram
-
-
-
?
KSKVLVVQPK + H2O
KSKVL + VVQPK
show the reaction diagram
P4-substituted peptide
-
-
?
KTAVLVVQPK + H2O
KTGVL + VVQPK
show the reaction diagram
P3-substituted peptide
-
-
?
KTDVLVVQPK + H2O
KTDVL + VVQPK
show the reaction diagram
P3-substituted peptide
-
-
?
KTFVLVVQPK + H2O
KTFVL + VVQPK
show the reaction diagram
P3-substituted peptide
-
-
?
KTGVLVVQPK + H2O
KTGVL + VVQPK
show the reaction diagram
P3-substituted peptide
-
-
?
KTKALVVQPK + H2O
KTKAL + VVQPK
show the reaction diagram
P2-substituted peptide
-
-
?
KTKDLVVQPK + H2O
KTKDL + VVQPK
show the reaction diagram
P2-substituted peptide
-
-
?
KTKFLVVQPK + H2O
KTKFL + VVQPK
show the reaction diagram
P2-substituted peptide
-
-
?
KTKGLVVQPK + H2O
KTKGL + VVQPK
show the reaction diagram
P2-substituted peptide
-
-
?
KTKILVVQPK + H2O
KTKIL + VVQPK
show the reaction diagram
P2-substituted peptide
-
-
?
KTKLLVVQPK + H2O
KTKLL + VVQPK
show the reaction diagram
P2-substituted peptide
-
-
?
KTKNLVVQPK + H2O
KTKNL + VVQPK
show the reaction diagram
P2-substituted peptide
-
-
?
KTKSLVVQPK + H2O
KTKSL + VVQPK
show the reaction diagram
P2-substituted peptide
-
-
?
KTKVAVVQPK + H2O
KTKVA + VVQPK
show the reaction diagram
P1-substituted peptide
-
-
?
KTKVDVVQPK + H2O
KTKVD + VVQPK
show the reaction diagram
P1-substituted peptide
-
-
?
KTKVFVVQPK + H2O
KTKVF + VVQPK
show the reaction diagram
P1-substituted peptide
-
-
?
KTKVGVVQPK + H2O
KTKVG + VVQPK
show the reaction diagram
P1-substituted peptide
-
-
?
KTKVLDVQPK + H2O
KTKVL + DVQPK
show the reaction diagram
P1'-substituted peptide
-
-
?
KTKVLFVQPK + H2O
KTKVL + FVQPK
show the reaction diagram
P1'-substituted peptide
-
-
?
KTKVLGVQPK + H2O
KTKVL + GVQPK
show the reaction diagram
P1'-substituted peptide
-
-
?
KTKVLIVQPK + H2O
KTKVL + IVQPK
show the reaction diagram
P1'-substituted peptide
-
-
?
KTKVLKVQPK + H2O
KTKVL + KVQPK
show the reaction diagram
P1'-substituted peptide
-
-
?
KTKVLLVQPK + H2O
KTKVL + LVQPK
show the reaction diagram
P1'-substituted peptide
-
-
?
KTKVLPVQPK + H2O
KTKVL + PVQPK
show the reaction diagram
P1'-substituted peptide
-
-
?
KTKVLSVQPK + H2O
KTKVL + SVQPK
show the reaction diagram
P1'-substituted peptide
-
-
?
KTKVLVVQPK + H2O
KTKVL + VVQPK
show the reaction diagram
KTKVMVVQPK + H2O
KTKVM + VVQPK
show the reaction diagram
P1-substituted peptide
-
-
?
KTKVSVVQPK + H2O
KTKVS + VVQPK
show the reaction diagram
P1-substituted peptide
-
-
?
KTKVYVVQPK + H2O
KTKVY + VVQPK
show the reaction diagram
P1-substituted peptide
-
-
?
KTLVLVVQPK + H2O
KTLVL + VVQPK
show the reaction diagram
P3-substituted peptide
-
-
?
KTSVLVVQPK + H2O
KTSVL + VVQPK
show the reaction diagram
P3-substituted peptide
-
-
?
KTVVLVVQPK + H2O
KTVVL + VVQPK
show the reaction diagram
P3-substituted peptide
-
-
?
KVKVLVVQPK + H2O
KVKVL + VVQPK
show the reaction diagram
P4-substituted peptide
-
-
?
KVLVVQPK + H2O
KVL + VVQPK
show the reaction diagram
-
-
-
?
PPAILPIISE + H2O
PPAIL + PIISE
show the reaction diagram
-
-
-
?
PPMVGVLDAP + H2O
PPMVG + VLDAP
show the reaction diagram
-
-
-
?
TKVLVVQPK + H2O
TKVL + VVQPK
show the reaction diagram
-
-
-
?
Val-Ser-Gln-Ala-Tyr-Pro-Ile-Val-Gln + H2O
Val-Ser-Gln-Ala-Tyr + Pro-Ile-Val-Gln
show the reaction diagram
-
-
-
-
?
Val-Ser-Gln-Asn-Tyr-Pro-Ile-Val-Gln + H2O
Val-Ser-Gln-Asn-Tyr + Pro-Ile-Val-Gln
show the reaction diagram
-
-
-
-
?
Val-Ser-Gln-Cys-Tyr-Pro-Ile-Val-Gln + H2O
Val-Ser-Gln-Cys-Tyr + Pro-Ile-Val-Gln
show the reaction diagram
-
-
-
-
?
Val-Ser-Gln-Gly-Tyr-Pro-Ile-Val-Gln + H2O
Val-Ser-Gln-Gly-Tyr + Pro-Ile-Val-Gln
show the reaction diagram
-
-
-
-
?
Val-Ser-Gln-Ile-Tyr-Pro-Ile-Val-Gln + H2O
Val-Ser-Gln-Ile-Tyr + Pro-Ile-Val-Gln
show the reaction diagram
-
-
-
-
?
Val-Ser-Gln-Leu-Tyr-Pro-Ile-Val-Gln + H2O
Val-Ser-Gln-Leu-Tyr + Pro-Ile-Val-Gln
show the reaction diagram
-
-
-
-
?
Val-Ser-Gln-Phe-Tyr-Pro-Ile-Val-Gln + H2O
Val-Ser-Gln-Phe-Tyr + Pro-Ile-Val-Gln
show the reaction diagram
-
-
-
-
?
Val-Ser-Gln-Thr-Tyr-Pro-Ile-Val-Gln + H2O
Val-Ser-Gln-Thr-Tyr + Pro-Ile-Val-Gln
show the reaction diagram
-
-
-
-
?
Val-Ser-Gln-Val-Tyr-Pro-Ile-Val-Gln + H2O
Val-Ser-Gln-Val-Tyr + Pro-Ile-Val-Gln
show the reaction diagram
-
-
-
-
?
VAQNYPIVQ + H2O
VAQNY + PIVQ
show the reaction diagram
-
Ala and Pro are preferred at position P4
-
-
?
VPQNYPIVQ + H2O
VPQNY + PIVQ
show the reaction diagram
-
Ala and Pro are preferred at position P4
-
-
?
VSANYPIVQ + H2O
VSANY + PIVQ
show the reaction diagram
-
Ala and Lys are preferred at position P3
-
-
?
VSKNYPIVQ + H2O
VSKNY + PIVQ
show the reaction diagram
-
Ala and Lys are preferred at position P3
-
-
?
VSQNFPIVQ + H2O
VSQNF + PIVQ
show the reaction diagram
-
highest preference for Leu at position P1, followed by Phe or Met
-
-
?
VSQNLPIVQ + H2O
VSQNL + PIVQ
show the reaction diagram
-
highest preference for Leu at position P1, followed by Phe or Met
-
-
?
VSQNMPIVQ + H2O
VSQNM + PIVQ
show the reaction diagram
-
highest preference for Leu at position P1, followed by Phe or Met
-
-
?
YDPPAILPII + H2O
YDPPAIL + PII
show the reaction diagram
YDPPAILPII + H2O
YDPPAIL + Pro-Ile-Ile
show the reaction diagram
additional information
?
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
Gag polyprotein + H2O
?
show the reaction diagram
Gag-Pol polyprotein + H2O
?
show the reaction diagram
additional information
?
-
-
the enzyme is responsible for processing both the initial translation products - precursors Gag-Pro-Pol, Gag-Pro and Gag into functional enzymes - protease, reverse transcriptase and integrase - and the mature structural proteins of the matrix, capsid and nucleocapsid
-
-
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
(NH4)2SO4
-
with YDPPAILPII as substrate, most active at 1-2 M NaCl or (NH4)2SO4
ammonium sulfate
-
activates
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
Ac-PQVL-azetidine-VM
-
IC50: 0.25 mM
Ac-PQVL-pipecolic acid-VM
-
IC50: 0.015 mM
Ac-Pro-Glu-Val-Leu-azetidine-Val-Met
-
IC50: 0.250 mM
Ac-Pro-Glu-Val-Leu-pipecolic acid-Val-Met
-
IC50: 0.015 mM
Ala-Pro-Gln-Val-Leu-r-Pro-Val-Met-His-Pro
-
Ala-Pro-Gln-Val-Sta-Val-Met-His-Pro
-
cerulenin
-
IC50: 5 mM
Gly-Val-Leu-Tyr-statine-Glu-Ala
-
IC50: 0.10 mM
HBY-793
a compound which inhibits EIAV PR
KH 164
modest inhibitor of MMLV PR
LP-149
inhibitor of FIV PR
Lys-Thr-Lys-Val-Leu-r-Val-Val-Gln-Pro-Lys
-
Lys-Thr-Lys-Val-Sta-Val-Gln-Pro-Gly
-
pepstatin A
-
IC50: 0.3-0.5 mM
PQV-statine-AI
-
IC50: 0.1 mM
-
Pro-Glu-Val-statine-Ala-Leu
-
IC50: 0.10 mM
UK 88.947
a compound which inhibits HIV-1PR
YDPPAI-statine-II
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.042
KAKVLVVQPK
P4-substitutedpeptide
0.048
KDKVLVVQPK
P4-substitutedpeptide
0.021
KGKVLVVQPK
P4-substituted peptide
0.019
KGPPVILPIQAP
-
pH 5.6, 37°C
0.03
KLKVLVVQPK
value below 0.03, P4-substituted peptide
0.01
KPKVLVVQPK
value below 0.01, P4-substituted peptide
0.022
KSKVLVVQPK
P4-substitutedpeptide
0.01
KTAVLVVQPK
value below 0.01, P3-substituted peptide
0.026
KTDVLVVQPK
P3-substituted peptide
0.042
KTFVLVVQPK
P3-substituted peptide
0.02
KTGVLVVQPK
value below 0.02, P3-substituted peptide
0.02
KTKALVVQPK
value below 0.02, P2-substituted peptide
0.043
KTKDLVVQPK
P2-substituted peptide
0.02
KTKFLVVQPK
value below 0.02, P2-substituted peptide
0.2
KTKGLVVQPK
P2-substituted peptide
0.01
KTKILVVQPK
value below 0.01, P2-substituted peptide
0.025
KTKLLVVQPK
P2-substituted peptide
0.033
KTKNLVVQPK
P2-substituted peptide
0.026
KTKSLVVQPK
P2-substituted peptide
0.01
KTKVAVVQPK
P1-substituted peptide
0.032
KTKVDVVQPK
P1-substituted peptide
0.048
KTKVFVVQPK
P1-substituted peptide
0.01
KTKVGVVQPK
value below 0.01, P1-substituted peptide
0.01
KTKVLFVQPK
value below 0.01, P1'-substituted peptide
0.021
KTKVLGVQPK
P1'-substituted peptide
0.021
KTKVLIVQPK
P1'-substituted peptide
0.13
KTKVLKVQPK
P1'-substituted peptide
0.021
KTKVLLVQPK
P1'-substituted peptide
0.063
KTKVLPVQPK
P1'-substituted peptide
0.016
KTKVLSVQPK
P1'-substituted peptide
0.006 - 0.18
KTKVLVVQPK
0.02
KTKVMVVQPK
value below 0.02, P1-substituted peptide
0.017
KTKVSVVQPK
P1-substituted peptide
0.014
KTKVYVVQPK
P1-substituted peptide
0.01
KTLVLVVQPK
value below 0.01, P3-substituted peptide
0.01
KTSVLVVQPK
value below 0.01, P3-substituted peptide
0.01
KTVVLVVQPK
value below 0.01, P3-substituted peptide
0.01
KVKVLVVQPK
value below 0.01, P4-substituted peptide
0.023
PPMVGVLDAP
-
pH 5.6, 37°C
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.07
APQVLPVMHP
bovine leukemia virus
-
pH 5.6, 37°C
0.22
KAKVLVVQPK
bovine leukemia virus
P10270
P4-substituted peptide
0.9
KDKVLVVQPK
bovine leukemia virus
P10270
P4-substituted peptide
0.58
KGKVLVVQPK
bovine leukemia virus
P10270
P4-substituted peptide
0.02
KGPPVILPIQAP
bovine leukemia virus
-
pH 5.6, 37°C
0.74
KLKVLVVQPK
bovine leukemia virus
P10270
P4-substituted peptide
0.16
KPKVLVVQPK
bovine leukemia virus
P10270
P4-substituted peptide
0.18
KQPAILVHTPG
bovine leukemia virus
-
pH 5.6, 37°C
0.19
KSKVLVVQPK
bovine leukemia virus
P10270
P4-substituted peptide
0.18
KTAVLVVQPK
bovine leukemia virus
P10270
P3-substituted peptide
0.17
KTDVLVVQPK
bovine leukemia virus
P10270
P3-substituted peptide
0.44
KTFVLVVQPK
bovine leukemia virus
P10270
P3-substituted peptide
0.74
KTGVLVVQPK
bovine leukemia virus
P10270
P3-substituted peptide
0.35
KTKALVVQPK
bovine leukemia virus
P10270
P2-substituted peptide
0.07
KTKDLVVQPK
bovine leukemia virus
P10270
P2-substituted peptide
0.32
KTKFLVVQPK
bovine leukemia virus
P10270
P2-substituted peptide
0.19
KTKGLVVQPK
bovine leukemia virus
P10270
P2-substituted peptide
0.29
KTKILVVQPK
bovine leukemia virus
P10270
P2-substituted peptide
0.29
KTKLLVVQPK
bovine leukemia virus
P10270
P2-substituted peptide
0.13
KTKNLVVQPK
bovine leukemia virus
P10270
P2-substituted peptide
0.35
KTKSLVVQPK
bovine leukemia virus
P10270
P2-substituted peptide
0.34
KTKVAVVQPK
bovine leukemia virus
P10270
P1-substituted peptide
0.11
KTKVDVVQPK
bovine leukemia virus
P10270
P1-substituted peptide
2
KTKVFVVQPK
bovine leukemia virus
P10270
P1-substituted peptide
0.09
KTKVGVVQPK
bovine leukemia virus
P10270
P1-substituted peptide
0.01
KTKVLDVQPK
bovine leukemia virus
P10270
value below 0.01, P1'-substituted peptide
0.28
KTKVLFVQPK
bovine leukemia virus
P10270
P1'-substituted peptide
0.12
KTKVLGVQPK
bovine leukemia virus
P10270
P1'-substituted peptide
0.23
KTKVLIVQPK
bovine leukemia virus
P10270
P1'-substituted peptide
0.36
KTKVLKVQPK
bovine leukemia virus
P10270
P1'-substituted peptide
0.34
KTKVLLVQPK
bovine leukemia virus
P10270
P1'-substituted peptide
0.85
KTKVLPVQPK
bovine leukemia virus
P10270
P1'-substituted peptide
0.18
KTKVLSVQPK
bovine leukemia virus
P10270
P1'-substituted peptide
0.003 - 0.27
KTKVLVVQPK
0.24
KTKVMVVQPK
bovine leukemia virus
P10270
P1-substituted peptide
0.11
KTKVSVVQPK
bovine leukemia virus
P10270
P1-substituted peptide
0.74
KTKVYVVQPK
bovine leukemia virus
P10270
P1-substituted peptide
0.11
KTLVLVVQPK
bovine leukemia virus
P10270
P3-substituted peptide
0.2
KTSVLVVQPK
bovine leukemia virus
P10270
P3-substituted peptide
0.13
KTVVLVVQPK
bovine leukemia virus
P10270
P3-substituted peptide
0.2
KVKVLVVQPK
bovine leukemia virus
P10270
P4-substituted peptide
0.71
KVLVVQPK
bovine leukemia virus
P10270
-
0.04
PPAILPIISE
bovine leukemia virus
-
pH 5.6, 37°C
0.01
PPMVGVLDAP
bovine leukemia virus
-
pH 5.6, 37°C
0.35
TKVLVVQPK
bovine leukemia virus
P10270
-
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.088
Ala-Pro-Gln-Val-Leu-r-Pro-Val-Met-His-Pro
-
0.181
Ala-Pro-Gln-Val-Sta-Val-Met-His-Pro
-
0.114
amprenavir
-
20
DMP-323
value above 20 mM
1
HBY-793
a compound which inhibits EIAV PR
9.475
indinavir
-
1.715
KH 164
modest inhibitor of MMLV PR
12.96
LP-149
inhibitor of FIV PR
0.013
Lys-Thr-Lys-Val-Leu-r-Val-Val-Gln-Pro-Lys
-
0.108
Lys-Thr-Lys-Val-Sta-Val-Gln-Pro-Gly
-
20
nelfinavir
value above 20 mM
11.47
ritonavir
-
20
saquinavir
value above 20 mM
20
UK 88.947
a compound which inhibits HIV-1PR
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.25
Ac-PQVL-azetidine-VM
bovine leukemia virus
-
IC50: 0.25 mM
0.015
Ac-PQVL-pipecolic acid-VM
bovine leukemia virus
-
IC50: 0.015 mM
0.25
Ac-Pro-Glu-Val-Leu-azetidine-Val-Met
bovine leukemia virus
-
IC50: 0.250 mM
0.015
Ac-Pro-Glu-Val-Leu-pipecolic acid-Val-Met
bovine leukemia virus
-
IC50: 0.015 mM
5
cerulenin
bovine leukemia virus
-
IC50: 5 mM
0.1
Gly-Val-Leu-Tyr-statine-Glu-Ala
bovine leukemia virus
-
IC50: 0.10 mM
0.3 - 0.5
pepstatin A
bovine leukemia virus
-
IC50: 0.3-0.5 mM
0.1
PQV-statine-AI
bovine leukemia virus
-
IC50: 0.1 mM
-
0.1
Pro-Glu-Val-statine-Ala-Leu
bovine leukemia virus
-
IC50: 0.10 mM
0.0005
YDPPAI-statine-II
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.25
-
reaction with YDPPAILPII
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
3.5 - 7.5
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0 - 80
-
active range
20 - 80
-
20°C: about 45% of maximal activity, 80°C: about 70% of maximal activity, reaction with YDPPAILPII
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
additional information
-
enzyme is purified from inclusion bodies of Escherichia coli
-
Manually annotated by BRENDA team
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
-
2 * 14000, SDS-PAGE
additional information
-
structure molecular modeling, S2 subsite sequence comparison
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
proteolytic modification
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5 - 6.5
-
the purified enzyme is more stable at pH 5.0 than at pH 6.5 due to the reduced autolytic activity at the C-terminus
668796
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
from recombinant inclusion bodies
-
native enzyme from viral particles under denaturing conditions, and recombinant enzyme from Escherichia coli
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
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the enzyme is cloned into pMal-c2 vector with N-terminal or with N- as well as C-terminal flanking sequences, and expressed in fusion with maltose binding protein. The proteinase self-processes itself from the fusion protein during expression and forms inclusion bodies
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
N38D
Km: 0.18 mM (KTKVLVVQPK), kcat: 0.023/sec (KTKVLVVQPK)
V57I
Km: 0.0075 mM (KTKVLVVQPK), kcat: 0.006/sec (KTKVLVVQPK)
V57I/L58G/A60I
Km: 0.03 mM (KTKVLVVQPK), kcat: 0.016/sec (KTKVLVVQPK)
W99V
Km: 0.006 mM (KTKVLVVQPK), kcat: 0.003/sec (KTKVLVVQPK)