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Literature summary for 1.11.1.6 extracted from

  • Rahi, A.; Rehan, M.; Garg, R.; Tripathi, D.; Lynn, A.M.; Bhatnagar, R.
    Enzymatic characterization of catalase from Bacillus anthracis and prediction of critical residues using information theoretic measure of relative entropy (2011), Biochem. Biophys. Res. Commun., 411, 88-95.
    View publication on PubMed
Search for more literature for 1.11.1.6

Cloned(Commentary)

Cloned (Comment) Organism
expression of wild-type and mutant His-tagged Cat1.4 isozymes in Escherichia coli strain BL21 (DE3) Bacillus anthracis

Protein Variants

Protein Variants Comment Organism
D270A site-directed mutagenesis Bacillus anthracis
H146A site-directed mutagenesis Bacillus anthracis
H215A site-directed mutagenesis Bacillus anthracis
H55A site-directed mutagenesis Bacillus anthracis
N376A site-directed mutagenesis Bacillus anthracis
N82A site-directed mutagenesis Bacillus anthracis
P391A site-directed mutagenesis Bacillus anthracis
Q332A site-directed mutagenesis Bacillus anthracis
R6A site-directed mutagenesis Bacillus anthracis
V210A site-directed mutagenesis Bacillus anthracis
W257A site-directed mutagenesis Bacillus anthracis
Y117A site-directed mutagenesis Bacillus anthracis
Y338A site-directed mutagenesis Bacillus anthracis
Y397A site-directed mutagenesis Bacillus anthracis

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
13.74
-
 H2O2 recombinant wild-type enzyme, pH 7.0, 25°C Bacillus anthracis

Metals/Ions

Metals/Ions Comment Organism Structure
Iron heme Bacillus anthracis

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
58000
-
 x * 58000, recombinant isozyme Cat1.4, SDS-PAGE Bacillus anthracis

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2 H2O2 Bacillus anthracis
-
 O2 + 2 H2O
-
 ?

Organism

Organism UniProt Comment Textmining
Bacillus anthracis
-
 isozyme Cat1.4
-

Purification (Commentary)

Purification (Comment) Organism
recombinanat wild-type and mutant His-tagged Cat1.4 isozymes from Escherichia coli strain BL21 (DE3) to homogeneity Bacillus anthracis

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2 H2O2
-
 Bacillus anthracis O2 + 2 H2O
-
 ?

Subunits

Subunits Comment Organism
? x * 58000, recombinant isozyme Cat1.4, SDS-PAGE Bacillus anthracis
More homology modeling of isozyme Cat1.4 Bacillus anthracis

Synonyms

Synonyms Comment Organism
Cat1.4
-
 Bacillus anthracis

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
25
-
 assay at Bacillus anthracis

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7
-
 assay at Bacillus anthracis

Cofactor

Cofactor Comment Organism Structure
heme
-
 Bacillus anthracis

General Information

General Information Comment Organism
additional information structure-function analysis, overview. H55 and Y338 in the active site are crucial for the activity. The distal heme ligand binding domain 46RERIPERVVHAKG58 encompasses the essential distal histidine residue, and the proximal heme ligand binding domain 334R-F-Y-D340 harbors the essential proximal tyrosine residue. Other catalase specific motifs are 126VGNNTP131, 107RDXRGFAXKFYT118, and 92RFSTV96. Tyr117 from sequence 107RDXRGFAXKFYT118 is crucial for activity Bacillus anthracis
physiological function catalase is responsible for the enzymatic destruction/detoxification of hydrogen peroxide, to combat its deleterious effects Bacillus anthracis