3.4.23.B8: human T-cell leukemia virus type 1 protease

This is an abbreviated version!
For detailed information about human T-cell leukemia virus type 1 protease, go to the full flat file.

Reaction

Processing at the authentic HIV-1 PR recognition site and release of the mature p17 matrix and the p24 capsid protein, as a result of the cleavage of the -SQNY-/-PIVQ- cleavage site. =

Synonyms

C2A HTLV-1 PR, HTLV-1 PR, HTLV-1 protease, HTLV-I PR, HTLV-I protease, human T cell leukemia virus PR, human T cell leukemia virus protease, human T-cell leukemia virus type 1 protease, human T-lymphotropic virus type I protease, More, retropepsin (human T-cell leukemia virus), simian T-cell leukemia virus endopeptidase

ECTree

     3 Hydrolases

         3.4 Acting on peptide bonds (peptidases)

             3.4.23 Aspartic endopeptidases

                3.4.23.B8 human T-cell leukemia virus type 1 protease

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Results	in table
2	AA Sequence
4	Application
1	CAS Registry Number
9	Cloned(Commentary)
8	Crystallization (Commentary)
6	General Information
68	IC50 Value
164	Inhibitors
11	kcat/KM [mM/s]
39	Ki Value [mM]
61	KM Value [mM]
1	Metals/Ions
5	Molecular Weight [Da]
5	Natural Substrates/ Products (Substrates)
38	Organism
5	pH Optimum
1	pH Range
1	Posttranslational Modification
25	Protein Variants
6	Purification (Commentary)
1	Reaction
1	Reaction Type
38	Reference
2	Renatured (Commentary)
2	Specific Activity [micromol/min/mg]
1	Storage Stability
130	Substrates and Products (Substrate)
10	Subunits
27	Synonyms
5	Temperature Optimum [°C]
66	Turnover Number [1/s]

Engineering

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Engineering on EC 3.4.23.B8 - human T-cell leukemia virus type 1 protease

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PROTEIN VARIANTS

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

A59I

Human T-cell leukemia virus type I

-

site-directed mutagenesis, highly reduced activity compared to the wild-type enzyme, no folding

669236

F67Q

Human T-cell leukemia virus type I

-

site-directed mutagenesis, inactive mutant, no folding

669236

L40I

4 entries

L49I

Human T-cell leukemia virus type I

-

autoproteolysis resistant mutant enzyme. KM-values and turnover-numbers are comparable to that of wild-type enzyme

647855

L57G

Human T-cell leukemia virus type I

-

site-directed mutagenesis, inactive mutant, no folding

669236

M37A

Human T-cell leukemia virus type I

-

site-directed mutagenesis, inactive mutant, no folding

669236

M37D

2 entries

M37I

Human T-cell leukemia virus type I

-

site-directed mutagenesis, reduced activity and highly reduced folding efficiency compared to the wild-type enzyme

669236

M37N

Human T-cell leukemia virus type I

-

site-directed mutagenesis, inactive mutant, no folding

669236

M37V

Human T-cell leukemia virus type I

-

site-directed mutagenesis, reduced activity and folding efficiency compared to the wild-type enzyme

669236

N96T

Human T-cell leukemia virus type I

-

site-directed mutagenesis, highly reduced activity compared to the wild-type enzyme, no folding

669236

N96T/N97P/W98V

Human T-cell leukemia virus type I

-

site-directed mutagenesis, inactive mutant, no folding

669236

N97P

Human T-cell leukemia virus type I

-

site-directed mutagenesis, highly reduced activity compared to the wild-type enzyme, no folding

669236

V56I

Human T-cell leukemia virus type I

-

site-directed mutagenesis, inactive mutant, no folding

669236

V56I/L57G/A59I

Human T-cell leukemia virus type I

-

site-directed mutagenesis, reduced activity and folding efficiency compared to the wild-type enzyme

669236

V56I/L57G/A59I/N96T/N97P/W98V

Human T-cell leukemia virus type I

-

site-directed mutagenesis, inactive mutant, no folding

669236

W98V

Human T-cell leukemia virus type I

-

site-directed mutagenesis, highly reduced activity compared to the wild-type enzyme, no folding

669236

additional information

4 entries

L40I

Human T-cell leukemia virus type I

-

site-directed mutagenesis, modified wild-type protease

667390

L40I

Human T-cell leukemia virus type I

-

protease used in the assay is an L40I mutant of the wild-type protease to prevent autolysis and improve stability

678624

L40I

Human T-cell leukemia virus type I

-

the mutation of the protease prevents autolysis and enhances enzyme stability and substrate cleavage

712764

L40I

Human T-cell leukemia virus type I

-

mutant used for inhibitor screening

717341

M37D

Human T-cell leukemia virus type I

-

site-directed mutagenesis, inactive mutant, no folding

669236

M37D

Human T-cell leukemia virus type I

P03362

mutation introduced to mimick HIV protease inhibitor binding site. Met37 is playing the vital role in ejection of HIV protease inhibitors from the binding pocket of HTLV protease

734513

additional information

Human T-cell leukemia virus type I

-

deletional analyses indicates that Asp38-Gly152 with an additional met-Pro sequence at the N-terminus is probably sufficient for the enzymatic activity, although the mature HTLV-1 protease consists of Pro33-Leu157. Pro148-Gly152 is important for the enzymatic activity, in addition to Gly143-Leu147 involved in the beta-sheet

647852

additional information

Human T-cell leukemia virus type I

-

construction of a L40I mutant enzyme lacking the 10 C-terminal amino acid residues, the mutant shows slightly increased activity compared to the wild-type enzyme

667390

additional information

Human T-cell leukemia virus type I

-

chemical synthesis of a full-length HTLV protease and a C-terminally truncated form encompassing residues 1-116. Constructs contain an S47C mutation for native chemical ligation and an L40I mutation that suppresses known autolysis of the protease without altering its catalytic activity. Truncation of the C-terminal tail lowers the turnover number of the viral enzyme by a factor of 2 and its catalytic efficiency by roughly tenfold

717390

additional information

Human T-cell leukemia virus type I

-

construction of C-terminally truncated forms of HTLV-1 protease of 116, 121 and 122 residues, with mutation L40I to prevent autoproteolysis. C-terminal residues are not essential for full activity

733121