BRENDA - Enzyme Database show
show all sequences of 3.4.22.66

Comparative site-directed mutagenesis in the catalytic amino acid triad in Calicivirus proteases

Oka, T.; Murakami, K.; Wakita, T.; Katayama, K.; Microbiol. Immunol. 55, 108-114 (2011)

Data extracted from this reference:

Engineering
Amino acid exchange
Commentary
Organism
C104S
site-directed mutagenesis, the mutant is affected in its catalytic activity of proteolytic processing
Rabbit hemorrhagic disease virus
C116S
site-directed mutagenesis, the mutant is affected in its catalytic activity of proteolytic processing
Sapporo virus
C122S
site-directed mutagenesis, the mutant is affected in its catalytic activity of proteolytic processing
feline calicivirus
C139S
site-directed mutagenesis, the mutant is affected in its catalytic activity of proteolytic processing
Norwalk virus
additional information
acidic amino acid (Glu or Asp), as well as the His and Cys in the putative catalytic triad, cannot be replaced by Ala for normal processing activity of the ORF1 polyprotein in vitro. Similarly, normal activity is not retained if the nucleophile Cys is replaced with Ser
feline calicivirus
additional information
acidic amino acid (Glu or Asp), as well as the His and Cys in the putative catalytic triad, cannot be replaced by Ala for normal processing activity of the ORF1 polyprotein in vitro. Similarly, normal activity is not retained if the nucleophile Cys is replaced with Ser
Norwalk virus
additional information
acidic amino acid (Glu or Asp), as well as the His and Cys in the putative catalytic triad, cannot be replaced by Ala for normal processing activity of the ORF1 polyprotein in vitro. Similarly, normal activity is not retained if the nucleophile Cys is replaced with Ser
Rabbit hemorrhagic disease virus
additional information
acidic amino acid (Glu or Asp), as well as the His and Cys in the putative catalytic triad, cannot be replaced by Ala for normal processing activity of the ORF1 polyprotein in vitro. Similarly, normal activity is not retained if the nucleophile Cys is replaced with Ser
Sapporo virus
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
feline calicivirus
-
FCV
-
Norwalk virus
-
NoV
-
Rabbit hemorrhagic disease virus
-
RHDV
-
Sapporo virus
-
SaV
-
Engineering (protein specific)
Amino acid exchange
Commentary
Organism
C104S
site-directed mutagenesis, the mutant is affected in its catalytic activity of proteolytic processing
Rabbit hemorrhagic disease virus
C116S
site-directed mutagenesis, the mutant is affected in its catalytic activity of proteolytic processing
Sapporo virus
C122S
site-directed mutagenesis, the mutant is affected in its catalytic activity of proteolytic processing
feline calicivirus
C139S
site-directed mutagenesis, the mutant is affected in its catalytic activity of proteolytic processing
Norwalk virus
additional information
acidic amino acid (Glu or Asp), as well as the His and Cys in the putative catalytic triad, cannot be replaced by Ala for normal processing activity of the ORF1 polyprotein in vitro. Similarly, normal activity is not retained if the nucleophile Cys is replaced with Ser
feline calicivirus
additional information
acidic amino acid (Glu or Asp), as well as the His and Cys in the putative catalytic triad, cannot be replaced by Ala for normal processing activity of the ORF1 polyprotein in vitro. Similarly, normal activity is not retained if the nucleophile Cys is replaced with Ser
Norwalk virus
additional information
acidic amino acid (Glu or Asp), as well as the His and Cys in the putative catalytic triad, cannot be replaced by Ala for normal processing activity of the ORF1 polyprotein in vitro. Similarly, normal activity is not retained if the nucleophile Cys is replaced with Ser
Rabbit hemorrhagic disease virus
additional information
acidic amino acid (Glu or Asp), as well as the His and Cys in the putative catalytic triad, cannot be replaced by Ala for normal processing activity of the ORF1 polyprotein in vitro. Similarly, normal activity is not retained if the nucleophile Cys is replaced with Ser
Sapporo virus
General Information
General Information
Commentary
Organism
additional information
acidic amino acid (Glu or Asp), as well as the His and Cys in the putative catalytic triad, cannot be replaced by Ala for normal processing activity of the ORF1 polyprotein in vitro. Similarly, normal activity is not retained if the nucleophile Cys is replaced with Ser
feline calicivirus
additional information
acidic amino acid (Glu or Asp), as well as the His and Cys in the putative catalytic triad, cannot be replaced by Ala for normal processing activity of the ORF1 polyprotein in vitro. Similarly, normal activity is not retained if the nucleophile Cys is replaced with Ser
Norwalk virus
additional information
acidic amino acid (Glu or Asp), as well as the His and Cys in the putative catalytic triad, cannot be replaced by Ala for normal processing activity of the ORF1 polyprotein in vitro. Similarly, normal activity is not retained if the nucleophile Cys is replaced with Ser
Rabbit hemorrhagic disease virus
additional information
acidic amino acid (Glu or Asp), as well as the His and Cys in the putative catalytic triad, cannot be replaced by Ala for normal processing activity of the ORF1 polyprotein in vitro. Similarly, normal activity is not retained if the nucleophile Cys is replaced with Ser
Sapporo virus
physiological function
the Calicivirus proteases cleaves the viral precursor polyprotein encoded by open reading frame1 into multiple intermediate and mature proteins. The Calicivirus protease is a Cys protease with catalytic Cys122, and the His39-Glu60-Cys122 catalytic triad formation is important for protease activity. The substrate recognition mechanism may be different between Caliciviridae, i.e. the Rabbit hemorrhagic disease virus and Sapporo virus proteases and the Norwalk virus and Feline calicivirus proteases. Proteolytic cleavage occurs at several cleavage sites in the ORF1 polyprotein without a functional acid residue in the FCV protease
feline calicivirus
physiological function
the Calicivirus proteases cleaves the viral precursor polyprotein encoded by open reading frame1 into multiple intermediate and mature proteins. The Calicivirus protease is a Cys protease with catalytic Cys139, and the His30-Glu54-Cys139 catalytic triad formation is important for protease activity. The substrate recognition mechanism may be different between Caliciviridae, i.e. the Rabbit hemorrhagic disease virus and Sapporo virus proteases and the Norwalk virus and Feline calicivirus proteases. Proteolytic cleavage occurs at several cleavage sites in the ORF1 polyprotein without a functional acid residue in the NoV protease
Norwalk virus
physiological function
the Calicivirus proteases cleaves the viral precursor polyprotein encoded by open reading frame1 into multiple intermediate and mature proteins. The Calicivirus protease is a Cys protease with catalytic Cys104, and the His27-Asp44-Cys104 catalytic triad formation is important for protease activity. The substrate recognition mechanism may be different between Caliciviridae, i.e. the Rabbit hemorrhagic disease virus and Sapporo virus proteases and the Norwalk virus and Feline calicivirus proteases. RHDV protease critically needs the acidic residue during catalysis
Rabbit hemorrhagic disease virus
physiological function
the Calicivirus proteases cleaves the viral precursor polyprotein encoded by open reading frame1 into multiple intermediate and mature proteins. The Calicivirus protease is a Cys protease with catalytic Cys116, and the His31-Glu52-Cys116 catalytic triad formation is important for protease activity. The substrate recognition mechanism may be different between Caliciviridae, i.e. the Rabbit hemorrhagic disease virus and Sapporo virus proteases and the Norwalk virus and Feline calicivirus proteases. SaV protease critically needs the acidic residue during catalysis
Sapporo virus
General Information (protein specific)
General Information
Commentary
Organism
additional information
acidic amino acid (Glu or Asp), as well as the His and Cys in the putative catalytic triad, cannot be replaced by Ala for normal processing activity of the ORF1 polyprotein in vitro. Similarly, normal activity is not retained if the nucleophile Cys is replaced with Ser
feline calicivirus
additional information
acidic amino acid (Glu or Asp), as well as the His and Cys in the putative catalytic triad, cannot be replaced by Ala for normal processing activity of the ORF1 polyprotein in vitro. Similarly, normal activity is not retained if the nucleophile Cys is replaced with Ser
Norwalk virus
additional information
acidic amino acid (Glu or Asp), as well as the His and Cys in the putative catalytic triad, cannot be replaced by Ala for normal processing activity of the ORF1 polyprotein in vitro. Similarly, normal activity is not retained if the nucleophile Cys is replaced with Ser
Rabbit hemorrhagic disease virus
additional information
acidic amino acid (Glu or Asp), as well as the His and Cys in the putative catalytic triad, cannot be replaced by Ala for normal processing activity of the ORF1 polyprotein in vitro. Similarly, normal activity is not retained if the nucleophile Cys is replaced with Ser
Sapporo virus
physiological function
the Calicivirus proteases cleaves the viral precursor polyprotein encoded by open reading frame1 into multiple intermediate and mature proteins. The Calicivirus protease is a Cys protease with catalytic Cys122, and the His39-Glu60-Cys122 catalytic triad formation is important for protease activity. The substrate recognition mechanism may be different between Caliciviridae, i.e. the Rabbit hemorrhagic disease virus and Sapporo virus proteases and the Norwalk virus and Feline calicivirus proteases. Proteolytic cleavage occurs at several cleavage sites in the ORF1 polyprotein without a functional acid residue in the FCV protease
feline calicivirus
physiological function
the Calicivirus proteases cleaves the viral precursor polyprotein encoded by open reading frame1 into multiple intermediate and mature proteins. The Calicivirus protease is a Cys protease with catalytic Cys139, and the His30-Glu54-Cys139 catalytic triad formation is important for protease activity. The substrate recognition mechanism may be different between Caliciviridae, i.e. the Rabbit hemorrhagic disease virus and Sapporo virus proteases and the Norwalk virus and Feline calicivirus proteases. Proteolytic cleavage occurs at several cleavage sites in the ORF1 polyprotein without a functional acid residue in the NoV protease
Norwalk virus
physiological function
the Calicivirus proteases cleaves the viral precursor polyprotein encoded by open reading frame1 into multiple intermediate and mature proteins. The Calicivirus protease is a Cys protease with catalytic Cys104, and the His27-Asp44-Cys104 catalytic triad formation is important for protease activity. The substrate recognition mechanism may be different between Caliciviridae, i.e. the Rabbit hemorrhagic disease virus and Sapporo virus proteases and the Norwalk virus and Feline calicivirus proteases. RHDV protease critically needs the acidic residue during catalysis
Rabbit hemorrhagic disease virus
physiological function
the Calicivirus proteases cleaves the viral precursor polyprotein encoded by open reading frame1 into multiple intermediate and mature proteins. The Calicivirus protease is a Cys protease with catalytic Cys116, and the His31-Glu52-Cys116 catalytic triad formation is important for protease activity. The substrate recognition mechanism may be different between Caliciviridae, i.e. the Rabbit hemorrhagic disease virus and Sapporo virus proteases and the Norwalk virus and Feline calicivirus proteases. SaV protease critically needs the acidic residue during catalysis
Sapporo virus
Other publictions for EC 3.4.22.66
No.
1st author
Pub Med
title
organims
journal
volume
pages
year
Activating Compound
Application
Cloned(Commentary)
Crystallization (Commentary)
Engineering
General Stability
Inhibitors
KM Value [mM]
Localization
Metals/Ions
Molecular Weight [Da]
Natural Substrates/ Products (Substrates)
Organic Solvent Stability
Organism
Oxidation Stability
Posttranslational Modification
Purification (Commentary)
Reaction
Renatured (Commentary)
Source Tissue
Specific Activity [micromol/min/mg]
Storage Stability
Substrates and Products (Substrate)
Subunits
Temperature Optimum [C]
Temperature Range [C]
Temperature Stability [C]
Turnover Number [1/s]
pH Optimum
pH Range
pH Stability
Cofactor
Ki Value [mM]
pI Value
IC50 Value
Activating Compound (protein specific)
Application (protein specific)
Cloned(Commentary) (protein specific)
Cofactor (protein specific)
Crystallization (Commentary) (protein specific)
Engineering (protein specific)
General Stability (protein specific)
IC50 Value (protein specific)
Inhibitors (protein specific)
Ki Value [mM] (protein specific)
KM Value [mM] (protein specific)
Localization (protein specific)
Metals/Ions (protein specific)
Molecular Weight [Da] (protein specific)
Natural Substrates/ Products (Substrates) (protein specific)
Organic Solvent Stability (protein specific)
Oxidation Stability (protein specific)
Posttranslational Modification (protein specific)
Purification (Commentary) (protein specific)
Renatured (Commentary) (protein specific)
Source Tissue (protein specific)
Specific Activity [micromol/min/mg] (protein specific)
Storage Stability (protein specific)
Substrates and Products (Substrate) (protein specific)
Subunits (protein specific)
Temperature Optimum [C] (protein specific)
Temperature Range [C] (protein specific)
Temperature Stability [C] (protein specific)
Turnover Number [1/s] (protein specific)
pH Optimum (protein specific)
pH Range (protein specific)
pH Stability (protein specific)
pI Value (protein specific)
Expression
General Information
General Information (protein specific)
Expression (protein specific)
KCat/KM [mM/s]
KCat/KM [mM/s] (protein specific)
732410
Kim
Broad-spectrum antivirals agai ...
Foot-and-mouth disease virus, Hepatovirus A, Human calicivirus Hu/NLV/GII/MD145-12/1987/US, Norwalk virus, SARS coronavirus, Transmissible gastroenteritis virus, Transmissible gastroenteritis virus Purdue
J. Virol.
86
11754-11762
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6
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2
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30
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13
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7
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6
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6
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24
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6
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2
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24
30
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7
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6
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6
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718084
Oka
Comparative site-directed muta ...
feline calicivirus, Norwalk virus, Rabbit hemorrhagic disease virus, Sapporo virus
Microbiol. Immunol.
55
108-114
2011
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8
8
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693255
Lee
Structural basis of inhibition ...
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284
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2009
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1
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1
1
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708950
Someya
Insights into the enzyme-subst ...
Chiba virus
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509-521
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1
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1
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1
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688730
Oka
Highly conserved configuration ...
feline calicivirus, Sapovirus
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81
6798-6806
2007
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2
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6
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670097
Zeitler
X-ray crystallographic structu ...
Norwalk virus
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2006
1
1
1
1
1
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2
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4
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670711
Asanaka
-
Replication and packaging of N ...
Norwalk virus
Proc. Natl. Acad. Sci. USA
19
10327-32
2006
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1
1
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1
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688725
Sosnovtsev
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Murine norovirus
J. Virol.
80
7816-7831
2006
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4
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1
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670082
Nakamura
A norovirus protease structure ...
Chiba virus
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2005
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1
1
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1
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670086
Belliot
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norovirus, norovirus MD145
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1
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671000
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Characterization of the norovi ...
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1
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1
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670075
Kuyumcu-Martinez
Calicivirus 3C-like proteinase ...
Enterovirus C, feline calicivirus, norovirus, norovirus MD145-12
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2004
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2
2
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Lambden
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Southampton virus
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1995
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647399
Lambden
Sequence and genome organizati ...
Southampton virus
Science
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1993
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