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

BRENDA support

Literature summary for 1.1.3.10 extracted from

  • Prongjit, M.; Sucharitakul, J.; Palfey, B.A.; Chaiyen, P.
    Oxidation mode of pyranose 2-oxidase is controlled by pH (2013), Biochemistry, 52, 1437-1445.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 1.1.3.10

Protein Variants

Protein Variants Comment Organism
T169A site-directed mutagenesis, the hydrogen bond between residue 169 and the N5 atom of FAD is absent, resulting in a change in the kinetic mechanism to one that consists of a ternary complex Trametes ochracea

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
 additional information steady-state and pre-steady-state kinetics, and kinetic isotope effects, of oxidative half-reaction and overall reaction, overview Trametes ochracea

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
D-glucose + O2 Trametes ochracea
-
 2-dehydro-D-glucose + H2O2
-
 ?
additional information Trametes ochracea pyranose 2-oxidase from Trametes multicolor is a flavoenzyme that catalyzes the oxidation of D-glucose and other aldopyranose sugars at the C2 position by using O2 as an electron acceptor to form the corresponding 2-oxo-sugars and H2O2 ?
-
 ?

Organism

Organism UniProt Comment Textmining
Trametes ochracea
-
-
-

Reaction

Reaction Comment Organism Reaction ID
D-glucose + O2 = 2-dehydro-D-glucose + H2O2 ping-pong reaction mechanism, but change in the enzyme kinetic mechanism from a ping-pong type mechanism at pH values below 7.0 to a ternary complex type mechanism at pH values above 7.0. The switching of reaction mechanism from the ping-pong to the ternary complex type may be resulting from the change of structural dynamics of the substrate loop in the T169A mutant or at higher pH values, overview Trametes ochracea
a

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
D-glucose + O2
-
 Trametes ochracea 2-dehydro-D-glucose + H2O2
-
 ?
additional information pyranose 2-oxidase from Trametes multicolor is a flavoenzyme that catalyzes the oxidation of D-glucose and other aldopyranose sugars at the C2 position by using O2 as an electron acceptor to form the corresponding 2-oxo-sugars and H2O2 Trametes ochracea ?
-
 ?

Synonyms

Synonyms Comment Organism
P2O
-
 Trametes ochracea
pyranose 2-Oxidase
-
 Trametes ochracea

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7
-
-
 Trametes ochracea

pH Range

pH Minimum pH Maximum Comment Organism
additional information
-
 flavin oxidation occurs via different pathways depending on the pH of the environment. At pH values lower than 8.0, the reduced enzyme reacts with O2 to form a C4a-hydroperoxyflavin intermediate, leading to elimination of H2O2. At pH 8.0 and higher, the majority of the reduced enzyme reacts with O2 via a pathway that does not allow detection of the C4a-hydroperoxyflavin, and flavin oxidation occurs with decreased rate constants upon the rise in pH. The switching between the two modes of enzyme oxidation is controlled by protonation of a group which has a pKa of 7.6, stopped-flow spectrophotometry, overview. The protonation of the group which controls the mode of flavin oxidation cannot be rapidly equilibrated with outside solvent. Using a double-mixing stopped-flow experiment, a rate constant for proton dissociation from the reaction site is determined to be 21.0 s-1 Trametes ochracea
5 10 activity range Trametes ochracea

Cofactor

Cofactor Comment Organism Structure
FAD flavoenzyme Trametes ochracea

General Information

General Information Comment Organism
additional information flavin oxidation occurs via different pathways depending on the pH of the environment. At pH values lower than 8.0, the reduced enzyme reacts with O2 to form a C4a-hydroperoxyflavin intermediate, leading to elimination of H2O2. At pH 8.0 and higher, the majority of the reduced enzyme reacts with O2 via a pathway that does not allow detection of the C4a-hydroperoxyflavin, and flavin oxidation occurs with decreased rate constants upon the rise in pH. The switching between the two modes of enzyme oxidation is controlled by protonation of a group which has a pKa of 7.6, stopped-flow spectrophotometry, overview Trametes ochracea