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Literature summary for 1.1.3.21 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)

Cloned (Comment) Organism
expressed in Escherichia coli, strain B834, pQE30 and pREP4 vectors Streptococcus sp.

Crystallization (Commentary)

Crystallization (Comment) Organism
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.

Protein Variants

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

Inhibitors

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

KM Value [mM]

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

Localization

Localization Comment Organism GeneOntology No. Textmining

Natural Substrates/ Products (Substrates)

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

Organism

Organism UniProt Comment Textmining
Streptococcus sp.
-
-
-

Purification (Commentary)

Purification (Comment) Organism
gel filtration, recombinant protein Streptococcus sp.

Specific Activity [micromol/min/mg]

Specific Activity Minimum [┬Ámol/min/mg] Specific Activity Maximum [┬Ámol/min/mg] Comment Organism
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)

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

Synonyms

Synonyms Comment Organism
GlpO protein
-
Streptococcus sp.

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
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.
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.
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

Cofactor Comment Organism Structure
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.