Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 1.11.1.19 extracted from

  • Wang, L.; Chang, A.; Yuan, W.; Bai, F.
    Recombinant expression, purification and characterization of a novel DyP-type peroxidase in Escherichia coli (2013), Chin. J. Biotechnol., 29, 772-784.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
expression in Escherichia coli Zymomonas mobilis

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
36000
-
3 * 36000, SDs-PAGE Zymomonas mobilis
108000
-
PAGE Zymomonas mobilis

Organism

Organism UniProt Comment Textmining
Zymomonas mobilis Q5NM63
-
-
Zymomonas mobilis ATCC 31821 Q5NM63
-
-

Purification (Commentary)

Purification (Comment) Organism
recombinant protein Zymomonas mobilis

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) + H2O2 + H+
-
Zymomonas mobilis ? + H2O
-
?
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) + H2O2 + H+
-
Zymomonas mobilis ATCC 31821 ? + H2O
-
?

Subunits

Subunits Comment Organism
trimer 3 * 36000, SDs-PAGE Zymomonas mobilis

Cofactor

Cofactor Comment Organism Structure
heme enzyme shows the typical Soret band Zymomonas mobilis