Pyruvate Oxidase

Modify Date: 2024-01-08 11:52:17

Pyruvate Oxidase Structure
Pyruvate Oxidase structure
Common Name Pyruvate Oxidase
CAS Number 9001-96-1 Molecular Weight N/A
Density N/A Boiling Point N/A
Molecular Formula N/A Melting Point N/A
MSDS USA Flash Point N/A

 Use of Pyruvate Oxidase


Pyruvate oxidase (PoxB) is a thiamine pyrophosphate-dependent oxidase that catalyzes the oxidative decarboxylation of pyruvate to acetyl phosphate, carbon dioxide and water. Pyruvate oxidase is an important enzyme in bacterial metabolism and is often used in biochemical research[1].

 Names

Name PYRUVATE OXIDASE
Synonym More Synonyms

 Pyruvate Oxidase Biological Activity

Description Pyruvate oxidase (PoxB) is a thiamine pyrophosphate-dependent oxidase that catalyzes the oxidative decarboxylation of pyruvate to acetyl phosphate, carbon dioxide and water. Pyruvate oxidase is an important enzyme in bacterial metabolism and is often used in biochemical research[1].
Related Catalog
References

[1]. Louis P Cornacchione, et al. Hydrogen peroxide-producing pyruvate oxidase from Lactobacillus delbrueckii is catalytically activated by phosphotidylethanolamine. BMC Microbiol. 2020 May 24;20(1):128.   

 Chemical & Physical Properties

Storage condition −20°C

 Safety Information

Personal Protective Equipment Eyeshields;Gloves;type N95 (US);type P1 (EN143) respirator filter
Safety Phrases 24/25
RIDADR NONH for all modes of transport
WGK Germany 3

 Articles33

More Articles
Alternating sites reactivity is a common feature of thiamin diphosphate-dependent enzymes as evidenced by isothermal titration calorimetry studies of substrate binding.

Biochemistry 52(15) , 2505-7, (2013)

Thiamin diphosphate (ThDP)-dependent enzymes play vital roles in cellular metabolism in all kingdoms of life. In previous kinetic and structural studies, a communication between the active centers in ...

A luminol chemiluminescence method for sensing histidine and lysine using enzyme reactions.

Anal. Biochem. 443(1) , 22-6, (2013)

The analysis of free amino acids in urine and plasma is useful for estimating disease status in clinical diagnoses. Changes in the concentration of free amino acids in foods are also useful markers of...

Using substrate analogues to probe the kinetic mechanism and active site of Escherichia coli MenD.

Biochemistry 50(40) , 8712-21, (2011)

MenD catalyzes the thiamin diphosphate-dependent decarboxylative carboligation of α-ketoglutarate and isochorismate. The enzyme is essential for menaquinone biosynthesis in many bacteria and has been ...

 Synonyms

EINECS 232-644-5