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Literature summary for 3.4.23.B8 extracted from

  • Kadas, J.; Weber, I.T.; Bagossi, P.; Miklossy, G.; Boross, P.; Oroszlan, S.; Toezser, J.
    Narrow substrate specificity and sensitivity toward ligand-binding site mutations of human T-cell Leukemia virus type 1 protease (2004), J. Biol. Chem., 279, 27148-27157.
    View publication on PubMed
Search for more literature for 3.4.23.B8

Cloned(Commentary)

Cloned (Comment) Organism
expression of wild-type and mutant enzymes as maltose-binding protein fusion proteins Human T-cell leukemia virus type I

Protein Variants

Protein Variants Comment Organism
A59I site-directed mutagenesis, highly reduced activity compared to the wild-type enzyme, no folding Human T-cell leukemia virus type I
F67Q site-directed mutagenesis, inactive mutant, no folding Human T-cell leukemia virus type I
L57G site-directed mutagenesis, inactive mutant, no folding Human T-cell leukemia virus type I
M37A site-directed mutagenesis, inactive mutant, no folding Human T-cell leukemia virus type I
M37D site-directed mutagenesis, inactive mutant, no folding Human T-cell leukemia virus type I
M37I site-directed mutagenesis, reduced activity and highly reduced folding efficiency compared to the wild-type enzyme Human T-cell leukemia virus type I
M37N site-directed mutagenesis, inactive mutant, no folding Human T-cell leukemia virus type I
M37V site-directed mutagenesis, reduced activity and folding efficiency compared to the wild-type enzyme Human T-cell leukemia virus type I
N96T site-directed mutagenesis, highly reduced activity compared to the wild-type enzyme, no folding Human T-cell leukemia virus type I
N96T/N97P/W98V site-directed mutagenesis, inactive mutant, no folding Human T-cell leukemia virus type I
N97P site-directed mutagenesis, highly reduced activity compared to the wild-type enzyme, no folding Human T-cell leukemia virus type I
V56I site-directed mutagenesis, inactive mutant, no folding Human T-cell leukemia virus type I
V56I/L57G/A59I site-directed mutagenesis, reduced activity and folding efficiency compared to the wild-type enzyme Human T-cell leukemia virus type I
V56I/L57G/A59I/N96T/N97P/W98V site-directed mutagenesis, inactive mutant, no folding Human T-cell leukemia virus type I
W98V site-directed mutagenesis, highly reduced activity compared to the wild-type enzyme, no folding Human T-cell leukemia virus type I

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
 additional information kinetics of wild-type and mutant enzymes Human T-cell leukemia virus type I

Metals/Ions

Metals/Ions Comment Organism Structure
NaCl activates at 4 M Human T-cell leukemia virus type I

Organism

Organism UniProt Comment Textmining
Human T-cell leukemia virus type I
-
 HTLV-I
-

Purification (Commentary)

Purification (Comment) Organism
recombinant enzyme from inclusion bodies Human T-cell leukemia virus type I

Renatured (Commentary)

Renatured (Comment) Organism
recombinant enzyme from inclusion bodies by dialysis Human T-cell leukemia virus type I

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
additional information
-
-
 Human T-cell leukemia virus type I

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
APQVLPVMHP + H2O
-
 Human T-cell leukemia virus type I APQVL + PVMHP
-
 ?
dabsyl-KTKVLVVQPK-EDANS + H2O i.e. peptide substrate IB268, fluorescent-labeled Human T-cell leukemia virus type I dabsyl-KTKVL + VVQPK-EDANS
-
 ?
DELILPVKRK + H2O
-
 Human T-cell leukemia virus type I DELIL + PVKRK
-
 ?
DKELYPLTSL + H2O low activity Human T-cell leukemia virus type I DKELY + PLTSL
-
 ?
DPASILPVIP + H2O
-
 Human T-cell leukemia virus type I DPASIL + PVIP
-
 ?
IPFAAAQQRK + H2O
-
 Human T-cell leukemia virus type I IPFAA + AQQRK
-
 ?
IQPLIMAVVNR + H2O good substrate Human T-cell leukemia virus type I IQPLIM + AVVNR
-
 ?
IRKILFLDG + H2O
-
 Human T-cell leukemia virus type I IRKIL + FLDG
-
 ?
IRQVLFLEKI + H2O good substrate Human T-cell leukemia virus type I IRQVL + FLEKI
-
 ?
KGPPVILPIQAP + H2O
-
 Human T-cell leukemia virus type I KGPPVIL + PIQAP
-
 ?
KTKVLVVQPK + H2O i.e. peptide substrate IB268, good substrate Human T-cell leukemia virus type I KTKVL + VVQPK
-
 ?
LTFTFPVVFMRR + H2O low activity Human T-cell leukemia virus type I LTFTF + PVVFMRR
-
 ?
additional information specificity of wild-type and mutant HTLV-1 PRs with diverse cleavage sites, overview Human T-cell leukemia virus type I ?
-
 ?
PKDIFPVTET + H2O
-
 Human T-cell leukemia virus type I PKDIF + PVTET
-
 ?
PLQVLTLNIERR + H2O
-
 Human T-cell leukemia virus type I PLQVL + TLNIERR
-
 ?
PPAILPIISE + H2O good substrate Human T-cell leukemia virus type I PPAIL + PIISE
-
 ?
PPMVGVLDAP + H2O
-
 Human T-cell leukemia virus type I PPMVG + VLDAP
-
 ?
PVVAMPVVIK + H2O
-
 Human T-cell leukemia virus type I PVVAM + PVVIK
-
 ?
RATVLTVALH + H2O
-
 Human T-cell leukemia virus type I RATVL + TVALH
-
 ?

Subunits

Subunits Comment Organism
More molecular structure modeling of wild-type enzyme with bound substrate KTKVLVVQPK Human T-cell leukemia virus type I

Synonyms

Synonyms Comment Organism
HTLV-I PR
-
 Human T-cell leukemia virus type I
HTLV-I protease
-
 Human T-cell leukemia virus type I
human T-cell leukemia virus type 1 protease
-
 Human T-cell leukemia virus type I

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
37
-
 assay at Human T-cell leukemia virus type I

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
5.6
-
 assay at Human T-cell leukemia virus type I