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Literature summary for 1.11.1.21 extracted from

  • Loewen, P.; Villanueva, J.; Switala, J.; Donald, L.; Ivancich, A.
    Unprecedented access of phenolic substrates to the heme active site of a catalase Substrate binding and peroxidase-like reactivity of Bacillus pumilus catalase monitored by X-ray crystallography and EPR spectroscopy (2015), Proteins, 83, 853-866 .
    View publication on PubMed
Search for more literature for 1.11.1.21

Crystallization (Commentary)

Crystallization (Comment) Organism
to 1.65-1.95 A resolution. One binding site in the main access channel and one site on the protein surface accommodate pyrogallol, catechol, resorcinol, guaiacol, hydroquinone, and 2-chlorophenol. A third site, in the heme distal side, accommodates only pyrogallol and catechol and interacts with the heme iron and the catalytic His and Arg residues Bacillus pumilus

Organism

Organism UniProt Comment Textmining
Bacillus pumilus
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2 H2O2
-
 Bacillus pumilus 2 H2O + O2
-
 ?
additional information for phenolic substrates, the phenolic oxygen is not directly coordinated to the heme iron. No substrates: pyrogallol, catechol, or hydroquinone Bacillus pumilus ?
-
 ?
peroxyacetic acid + 2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid)
-
 Bacillus pumilus ?
-
 ?

Subunits

Subunits Comment Organism
? x * 58000, SDS-PAGE Bacillus pumilus

Synonyms

Synonyms Comment Organism
BW16_04845
-
 Bacillus pumilus

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
339000
-
 H2O2 pH 7.0, 37°C Bacillus pumilus

Cofactor

Cofactor Comment Organism Structure
heme one pentacoordinated heme b per subunit, residue Tyr340 is the axial ligand Bacillus pumilus