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Synonyms
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pyruvate oxidase
no activity in Streptococcus pyogenes
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SpxB
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pyruvate + CoA + O2 = acetyl-CoA + CO2 + H2O2
pyruvate + CoA + O2 = acetyl-CoA + CO2 + H2O2
enzyme catalyzes transacetylation from pyruvate to CoA by an oxidase reaction in which H2O2 is produced
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pyruvate + CoA + O2 = acetyl-CoA + CO2 + H2O2
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pyruvate:oxygen 2-oxidoreductase (CoA-acetylating)
A flavoprotein (FAD). May be identical with EC 1.2.7.1 pyruvate synthase.
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62213-57-4
may be identical with EC 1.2.7.1
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pyruvate + CoA + O2
acetyl-CoA + CO2 + H2O2
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Substrates: -
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additional information
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Ala282Thr mutation in strain D39 reduces SpxB activity, probably by reducing FAD binding
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additional information
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activity is not enhanced by phosphatidyl-choline, -inositol, and -ethanolamine or by artificial electron acceptors
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additional information
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the trans-acting spxR regulatory gene positively regulates SpxB transcription in response to energy and metabolic state
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Whooping Cough
Purification and characterization of fimbriae isolated from Bordetella pertussis.
Whooping Cough
Purification and characterization of serotype 6 fimbriae from Bordetella pertussis and comparison of their properties with serotype 2 fimbriae.
Whooping Cough
Purification of serotype 2 fimbriae of Bordetella pertussis and their identification as a mouse protective antigen.
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no activity in Streptococcus pyogenes
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serotype 2
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the H2O2 produced by pyruvate oxidase activity inhibits growth of Staphylococcus aureus
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the H2O2 produced by pyruvate oxidase activity inhibits growth of Staphylococcus aureus
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the H2O2 produced by pyruvate oxidase activity inhibits growth of Staphylococcus aureus
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Highest Expressing Human Cell Lines
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Cell Line Links
Gene Links
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G389D
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spxB2 mutant, reduces H2O2 production to approximately that of a DELTAspxB null mutant. SpxB2 mutant shows an opaque colony phenotype and decreased production of H2O2
P449L
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spxB4 mutant, reduces H2O2 production to approximately that of a DELTAspxB null mutant. SpxB4 mutant shows an opaque colony phenotype and decreased production of H2O2
additional information
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deletion of the spxB gene. no pyruvate oxidase activity and no inhibition of Staphylococcus growth
additional information
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cis-acting mutations in spxB decrease H2O2 production. SpxB1 mutant with a 7 bp deletion (Datagaga) of one repeat unit of an adjacent direct repeat centres 136 bp upstream from the translation start codon of SpxB. SpxB1 mutant shows an opaque colony phenotype and decreased production of H2O2. SpxB transcript is greatly reduced (14fold) in the spxB1 mutant compared with parent strain D39. DELTAspxB deletion/insertion mutant, which forms large, opaque colonies on TSA plates similar to those of the spxB2 mutant, produces a minimal basal level of H2O2, and synthesizes capsule
additional information
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knockout of the spxB gene in strain D39 abolishes spontaneous transformation. Significant reduced expression levels of comC and recA as well as DNA release from bacterial cells during the early growth phase, coincident with the time of spontaneous competence in the parent strain. Supplementation with competencestimulating peptide 1 restores transformation. Neither supplementation with competencestimulating peptide 1 nor supplementation with the SpxB products H2O2 and acetate alteres DNA release. Supplementation of the parent strain with catalase does not reduce DNA release significantly
additional information
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deletion of the spxB gene. no pyruvate oxidase activity and no inhibition of Staphylococcus growth
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additional information
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deletion of the spxB gene. no pyruvate oxidase activity and no inhibition of Staphylococcus growth
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ammonium sulfate, hydroxyapatite, partially purified
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expressed in Escherichia coli
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additional information
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pneumococcal spxB gene influences competence, the mechanism remains elusive
additional information
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spxB transcription is regulated by both cis- and trans-acting regulatory elements
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Takeuchi, T.; Weinbach, E.C.; Diamond, L.S.
Pyruvate oxidase (CoA acetylating) in Entamoeba histolytica
Biochem. Biophys. Res. Commun.
65
591-596
1975
Entamoeba histolytica
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Seki, M.; Iida, K.; Saito, M.; Nakayama, H.; Yoshida, S.
Hydrogen peroxide production in Streptococcus pyogenes: involvement of lactate oxidase and coupling with aerobic utilization of lactate
J. Bacteriol.
186
2046-2051
2004
no activity in Streptococcus pyogenes
brenda
Regev-Yochay, G.; Trzcinski, K.; Thompson, C.M.; Malley, R.; Lipsitch, M.
Interference between Streptococcus pneumoniae and Staphylococcus aureus: In vitro hydrogen peroxide-mediated killing by Streptococcus pneumoniae
J. Bacteriol.
188
4996-5001
2006
Streptococcus pneumoniae, Streptococcus pneumoniae PN-20, Streptococcus pneumoniae Rx1
brenda
Baettig, P.; Muehlemann, K.
Influence of the spxB gene on competence in Streptococcus pneumoniae
J. Bacteriol.
190
1184-1189
2008
Streptococcus pneumoniae D39
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Ramos-Montanez, S.; Tsui, H.C.; Wayne, K.J.; Morris, J.L.; Peters, L.E.; Zhang, F.; Kazmierczak, K.M.; Sham, L.T.; Winkler, M.E.
Polymorphism and regulation of the spxB (pyruvate oxidase) virulence factor gene by a CBS-HotDog domain protein (SpxR) in serotype 2 Streptococcus pneumoniae
Mol. Microbiol.
67
729-746
2008
Streptococcus pneumoniae D39
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