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Literature summary for 1.11.1.21 extracted from

  • Varnado, C.L.; Hertwig, K.M.; Thomas, R.; Roberts, J.K.; Goodwin, D.C.
    Properties of a novel periplasmic catalase-peroxidase from Escherichia coli O157:H7 (2004), Arch. Biochem. Biophys., 421, 166-174.
    View publication on PubMed
Search for more literature for 1.11.1.21

Cloned(Commentary)

Cloned (Comment) Organism
expressed in Escherichia coli BL-21 DE3 pLysS cells Escherichia coli

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
3
-
 2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid) in 50 mM acetate buffer, pH 5.0, at 23°C Escherichia coli
27
-
 H2O2 in 100 mM phosphate buffer, pH 7.0, at 23°C Escherichia coli

Localization

Localization Comment Organism GeneOntology No. Textmining
periplasm
-
 Escherichia coli
-
-

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-

Purification (Commentary)

Purification (Comment) Organism
Ni-NTA column chromatography and phenyl-Sepharose column chromatography Escherichia coli

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid) + H2O2 KatP has stronger catalase than peroxidase activity Escherichia coli oxidized 2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid) + H2O
-
 ?
H2O2 KatP has stronger catalase than peroxidase activity Escherichia coli O2 + H2O
-
 ?

Synonyms

Synonyms Comment Organism
KatP
-
 Escherichia coli

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
77
-
 2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid) in 50 mM acetate buffer, pH 5.0, at 23°C Escherichia coli
18000
-
 H2O2 in 100 mM phosphate buffer, pH 7.0, at 23°C Escherichia coli

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
4.7
-
 maximal peroxidase activity Escherichia coli
7.2
-
 maximal catalase activity Escherichia coli

Cofactor

Cofactor Comment Organism Structure
heme ferric KatP possesses a mixture of pentacoordinate and hexacoordinate high-spin heme iron Escherichia coli

General Information

General Information Comment Organism
physiological function periplasmic catalase-peroxidases contributes to bacterial virulence Escherichia coli

kcat/KM [mM/s]

kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
26
-
 2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid) in 50 mM acetate buffer, pH 5.0, at 23°C Escherichia coli
640
-
 H2O2 in 100 mM phosphate buffer, pH 7.0, at 23°C Escherichia coli