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IUBMB Comments A flavoprotein (FAD). This bacterial enzyme participates in degradation of certain C -glucosides by catalysing the oxidation of the hydroxyl group at position 3 of the glycose moiety. The enzyme was found active with assorted C -glycosides, such as carminate, mangiferin, and C 6 D -glucose or C 8
Synonyms CarA ,
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C-glycoside 3-oxidase
BBE36490
-
CarA
-
-
-
-
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carminate + O2 = 3'-dehydrocarminate + H2O2
-
-
-
-
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carminate:oxygen 3'-oxidoreductase (H2O2-forming)
A flavoprotein (FAD). This bacterial enzyme participates in degradation of certain C-glucosides by catalysing the oxidation of the hydroxyl group at position 3 of the glycose moiety. The enzyme was found active with assorted C-glycosides, such as carminate, mangiferin, and C6-glycosylated flavonoids, but not with D-glucose or C8-glycosylated flavonoids.
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carminate + O2
3'-dehydrocarminate + H2O2
homoorientin + O2
3'-keto-homoorientin + H2O2
BBE36490
Substrates: -
?
isovitexin + O2
3'-keto-isovitexin + H2O2
BBE36490
Substrates: -
?
mangiferin + O2
3'-keto-magniferin + H2O2
BBE36490
Substrates: -
?
additional information
?
-
BBE36490
Substrates: the enzyme alsoshows broad substrate specificities toward O-glycosides, the specific activities are 100 to 1000 times lower than those of C-glycosides. No activity with D-glucose or C8-glycosylated flavonoids
?
carminate + O2
3'-dehydrocarminate + H2O2
BBE36490
Substrates: initial enzyme for carminic acid metabolism
?
carminate + O2
3'-dehydrocarminate + H2O2
BBE36490
Substrates: -
?
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carminate + O2
3'-dehydrocarminate + H2O2
BBE36490
Substrates: initial enzyme for carminic acid metabolism
?
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FAD
BBE36490
flavoprotein. One FAD would bind one CarA monomer
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(NH4)2S2O8
BBE36490
1 mM, 50% inhibition
Al2+
BBE36490
1 mM, 88% inhibition
-
aminoguanidine
BBE36490
1 mM, 9% inhibition
Ca2+
BBE36490
1 mM, 64% inhibition
carminate
BBE36490
substrate inhibition
Co2+
BBE36490
1 mM, 72% inhibition
Cu2+
BBE36490
1 mM, 86% inhibition
diethyldithiocarbamate
BBE36490
1 mM, 11% inhibition
Fe2+
BBE36490
1 mM, complete inhibition
Fe3+
BBE36490
1 mM, 54% inhibition
Hg2+
BBE36490
1 mM, complete inhibition
KCN
BBE36490
1 mM, 23% inhibition
NaN3
BBE36490
1 mM, 12% inhibition
p-chloromercuribenzoate
BBE36490
1 mM, 58% inhibition
Pb2+
BBE36490
1 mM, 42% inhibition
phenazine methosulfate
BBE36490
1 mM, 9% inhibition
phenylhydrazine
BBE36490
1 mM, 11% inhibition
Sr2+
BBE36490
1 mM, 89% inhibition
Zn2+
BBE36490
1 mM, 74% inhibition
additional information
BBE36490
5,5'-dithio-bis-2-nitrobenzoate, N-ethylmaleimide, and iodoacetate have no significant effect on activity
-
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0.019
carminate
BBE36490
pH 8.0, 28°C
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4.3
carminate
BBE36490
pH 8.0, 28°C
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0.7
carminate
BBE36490
pH 8.0, 28°C
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19.9
BBE36490
pH 8.0, 28°C
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6.5 - 10
BBE36490
pH 6.5: about 75% of maximal activity, pH 10.0: about 50% of maximal activity
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20 - 50
BBE36490
20°C: about 20% of maximal activity, 50°C: about 15% of maximal activity
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-
BBE36490
GenBank
brenda
Highest Expressing Human Cell Lines
Filter by:
Cell Line Links
Gene Links
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metabolism
BBE36490
the enzyme plays a crucial role in the metabolism of C-glycosides
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CGLYO_MICTR
515
0
54747
Swiss-Prot
other Location (Reliability: 2 )
CGLYO_ARTG1
Arthrobacter globiformis (strain ATCC 8010 / DSM 20124 / JCM 1332 / NBRC 12137 / NCIMB 8907 / NRRL B-2979 / 168)
519
0
55257
Swiss-Prot
-
CGLYO_MICSX
Microbacterium sp
501
0
52317
Swiss-Prot
-
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54900
BBE36490
gel filtration
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monomer
BBE36490
1 * 52300, calculated from sequence
monomer
BBE36490
1 * 50000, SDS-PAGE
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hanging-drop vapor-diffusion method
BBE36490
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H429A
BBE36490
inactive mutant enzyme
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4.2 - 11.4
BBE36490
28°C, 10 min, stable
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30
BBE36490
pH 8.0, 10 min, stable
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Kumano, T.; Hori, S.; Watanabe, S.; Terashita, Y.; Yu, H.Y.; Hashimoto, Y.; Senda, T.; Senda, M.; Kobayashi, M.
FAD-dependent C-glycoside-metabolizing enzymes in microorganisms Screening, characterization, and crystal structure analysis
Proc. Natl. Acad. Sci. USA
118
e2106580118
2021
Microbacterium sp. 5-2b (BBE36490)
brenda
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