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Literature summary extracted from

  • Colussi, T.; Parsonage, D.; Boles, W.; Matsuoka, T.; Mallett, T.C.; Karplus, P.A.; Claiborne, A.
    Structure of alpha-glycerophosphate oxidase from Streptococcus sp.: a template for the mitochondrial alpha-glycerophosphate dehydrogenase (2008), Biochemistry, 47, 965-977.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.1.3.21 expressed in Escherichia coli, strain B834, pQE30 and pREP4 vectors Streptococcus sp.
1.1.5.3 deletion mutant of Streptococcus sp. GlpO (GlpODELTA, lacking a 50-residue insert that includes a flexible surface region) is expressed in Escherichia coli Streptococcus sp.

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
1.1.3.21 intact GlpO structure, refined at 2.4 A resolution and structure of a deletion mutant lacking 50-residue insert, refined at 2.3 A resolution, multiwavelength anomalous dispersion data Streptococcus sp.
1.1.5.3 structure of a deletion mutant of Streptococcus sp. GlpO (GlpODELTA, lacking a 50-residue insert that includes a flexible surface region) is determined using multiwavelength anomalous dispersion data and refined at 2.3 A resolution Streptococcus sp.

Protein Variants

EC Number Protein Variants Comment Organism
1.1.3.21 additional information deletion mutant, 50-residue insert lacked consisting of residues Asp356-Ala405 including a flexible surface region Streptococcus sp.

Inhibitors

EC Number Inhibitors Comment Organism Structure
1.1.3.21 carboxylate structural characterization of enzyme-inhibitor interaction Streptococcus sp.

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.1.3.21 0.052
-
O2 pH 7.0, 5°C, wild-type enzyme, intact Streptococcus sp.
1.1.3.21 0.069
-
O2 pH 7.0, 5°C, wild-type enzyme, nicked Streptococcus sp.
1.1.3.21 0.46
-
O2 pH 7.0, 5°C, recombinant deletion mutant Streptococcus sp.
1.1.3.21 1.9
-
sn-glycerol 3-phosphate pH 7.0, 5°C, wild-type enzyme, intact Streptococcus sp.
1.1.3.21 1.9
-
sn-glycerol 3-phosphate intact enzyme form, at pH 7.0 and 25°C Streptococcus sp.
1.1.3.21 6.6
-
sn-glycerol 3-phosphate pH 7.0, 5°C, recombinant deletion mutant Streptococcus sp.
1.1.3.21 6.6
-
sn-glycerol 3-phosphate deletion mutant GlpODELTA, at pH 7.0 and 25°C Streptococcus sp.
1.1.3.21 36.2
-
sn-glycerol 3-phosphate pH 7.0, 5°C, wild-type enzyme, nicked Streptococcus sp.
1.1.3.21 36.2
-
sn-glycerol 3-phosphate nicked enzyme form, at pH 7.0 and 25°C Streptococcus sp.

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.1.3.21 sn-glycerol-3-phosphate + O2 Streptococcus sp. structural characterization, substrate binding site glycerone phosphate + H2O2
-
?

Organism

EC Number Organism UniProt Comment Textmining
1.1.3.21 Streptococcus sp.
-
-
-
1.1.5.3 Streptococcus sp.
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.1.3.21 gel filtration, recombinant protein Streptococcus sp.
1.1.5.3 deletion mutant of Streptococcus sp. GlpO (GlpODELTA, lacking a 50-residue insert that includes a flexible surface region) Streptococcus sp.

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
1.1.3.21 additional information
-
structural characterization, wild-type and deletion mutant, FAD- and substrate binding sites identified, active-site overlays, residues interacting with the amino acid substrate or with inhibitor carboxylate identified, structural and functional divergence between alpha-glycerophosphate oxidase (GlpO) and the bacterial and mitochondrial alpha-glycerophosphate dehydrogenases (GlpDs) discussed Streptococcus sp.

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.1.3.21 sn-glycerol 3-phosphate + O2
-
Streptococcus sp. glycerone phosphate + H2O2
-
r
1.1.3.21 sn-glycerol-3-phosphate + O2 structural characterization, substrate binding site Streptococcus sp. glycerone phosphate + H2O2
-
?

Synonyms

EC Number Synonyms Comment Organism
1.1.3.21 GlpO protein
-
Streptococcus sp.
1.1.5.3 GlpO
-
Streptococcus sp.

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
1.1.3.21 11.2
-
sn-glycerol 3-phosphate 10 microM enzyme and 0.77 mM O2, substrate concentration ranges between 2.5 and 50 mM, pH 7.0, 5°C, recombinant deletion mutant Streptococcus sp.
1.1.3.21 14.1
-
sn-glycerol 3-phosphate 10 microM enzyme and 0.77 mM O2, substrate concentration ranges between 2.5 and 50 mM, pH 7.0, 5°C, wild-type enzyme, nicked Streptococcus sp.
1.1.3.21 17.9
-
sn-glycerol 3-phosphate 10 microM enzyme and 0.77 mM O2, substrate concentration ranges between 2.5 and 50 mM, pH 7.0, 5°C, wild-type enzyme, intact Streptococcus sp.

Cofactor

EC Number Cofactor Comment Organism Structure
1.1.3.21 FAD the first two domains of the GlpO protein fold involved in FAD binding, linkage of substrate-binding domain to a beta-beta-alpha element of the FAD-binding domain Streptococcus sp.
1.1.5.3 FAD dependent on Streptococcus sp.