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G9637

Sigma-Aldrich

Glycerol 3-phosphate Oxidase from Pediococcus sp.

lyophilized powder, 40-80 units/mg solid, pH 8.1

Synonym(s):

sn-Glycerol 3-phosphate:oxygen 2-oxidoreductase, L-Glycerol 3-phosphate Oxidase

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About This Item

CAS Number:
9046-28-0
EC Number:
1.1.3.21 (BRENDA, IUBMB)
EC Number:
232-932-0
MDL number:
MFCD00131209
UNSPSC Code:
12352204
NACRES:
NA.54

biological source

bacterial (Pediococcus spp.)

Quality Level

200

form

lyophilized powder

specific activity

40-80 units/mg solid, pH 8.1

mol wt

~76 kDa (gel filtration)

storage temp.

2-8°C

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General description

Glycerol 3-phosphate Oxidase is a FAD-dependent α-glycerophosphate oxidase and catalyzes the formation of dihydroxyacetonephosphate. Glycerol 3-phosphate oxidase comprises of a flavin adenine dinucleotide (FAD) and a substrate binding domain and corresponds to molecular weight of 42 kDa. It exists as a monomer and the active site comprises of isoalloxazine ring and histidine 53, arginine 316 and lysine 345 residues crucial for ligand binding.

Application

Glycerol 3-phosphate Oxidase from Pediococcus sp. has been used in the kinetic assay to study gluconeogenesis in liver and in immobilization studies on pencil graphite (PG) electrode.
This enzyme is useful for enzymatic determination of triglyceride when coupled with lipoprotein lipase (LPL-311, LPL-314) and glycerokinase (GYK-301, GYK-311) in clinical analysis.

Physical properties

Isoelectric point : 4.1 -/+0.1
Michaelis constants : 3.2x10 -3M (L-α-Glycerophosphate), 6.8 x 10 -3M (D, L-form)
Inhibitors : Ionic detergents (SDS, LBS, etc.), Hg++, Ag+
Optimum pH : 8.0 - 8.5Optimum temperature : 35 - 40oC
pH Stability : pH 6.5 - 8.5 (25oC, 20hr) Thermal stability : below 40oC (pH 7.0, 15min)
Substrate specificity : The enzyme has the highest specificity for L-form of a-γlycerophosphate

Unit Definition

One unit will oxidize 1.0 μmole of L-glycerol 3-phosphate to dihydroxyacetone phosphate with the formation of H2O2 per min at 37°C, at the appropriate pH.

Physical form

Lyophilized powder containing stabilizers

Pictograms

Health hazard
GHS08

Signal Word

Danger

Hazard Statements

H334

Precautionary Statements

P261 - P284 - P501

Hazard Classifications

Resp. Sens. 1

Storage Class Code

11 - Combustible Solids

WGK

WGK 3

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable

Personal Protective Equipment

dust mask type N95 (US), Eyeshields, Gloves

Regulatory Listings

Regulatory Listings are mainly provided for chemical products. Only limited information can be provided here for non-chemical products. No entry means none of the components are listed. It is the user’s obligation to ensure the safe and legal use of the product.

JAN Code

G9637-BULK:
G9637-100UN:
G9637-500UN:
G9637-VAR:

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Certificates of Analysis (COA)

Lot/Batch Number
SLCG3592
SLCC6407
SLBW8064
SLBT5131
SLBS0462V

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Fabrication of glycerol biosensor based on co-immobilization of enzyme nanoparticles onto pencil graphite electrode
Narwal V and Pundir CS
Analytical Biochemistry, 555, 94-103 (2018)
Crystal structure of the flavoenzyme PA4991 from Pseudomonas aeruginosa
Jacewicz A, et al.
Acta Crystallographica. Section F, Structural Biology Communications, 72(2), 105-111 (2016)
Structure of alpha-glycerophosphate oxidase from Streptococcus sp.: a template for the mitochondrial alpha-glycerophosphate dehydrogenase
Colussi T, et al.
Biochemistry, 47(3), 965-977 (2008)
Characterization of glycerol phosphate oxidase from Streptococcus pneumoniae and its application for ketose synthesis
Li Z, et al.
Bioorganic & medicinal chemistry letters, 25(3), 504-507 (2015)
Effect of increasing levels of glycerin on growth rate, carcass traits and liver gluconeogenesis in young bulls
Ladeira MM, et al.
Anim. Feed Sci. Technol., 219, 241-248 (2016)
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Protocols

Enzymatic assay of lipase type XIII from Pseudomonas sp. using a coupled enzyme system of glycerol kinase and glycerophosphate oxidase (EC 3.1.1.3)

Enzymatic assay of lipase type XIII from Pseudomonas sp. using a coupled enzyme system of glycerol kinase and glycerophosphate oxidase (EC 3.1.1.3)

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