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Literature summary extracted from

  • Jonczyk, R.; Schmidt, H.; Osterrieder, A.; Fiesselmann, A.; Schullehner, K.; Haslbeck, M.; Sicker, D.; Hofmann, D.; Yalpani, N.; Simmons, C.; Frey, M.; Gier, A.
    Elucidation of the final reactions of DIMBOA-glucoside biosynthesis in maize: Characterization of Bx6 and Bx7 (2008), Plant Physiol., 146, 1053-1063.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
2.1.1.241 DNA and amino acid sequence determination and analysis, Bx7 maps to the cluster of Bx genes on the short arm of chromosome 4, Bx7 is located 9 cM distal to the marker adh2 at position 47, phylogenetic analysis, expression as His-tagged enzyme in Escherichia coli Zea mays

Inhibitors

EC Number Inhibitors Comment Organism Structure
2.1.1.241 additional information 1 mM Mg2+, 1 mM EDTA, 5% ethanol, or 6% DMSO have no effect on BX7 activity Zea mays

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.14.11.59 0.07
-
2-oxoglutarate in 100 mM potassium phosphate buffer (pH 7.0), at 30°C Zea mays
1.14.11.59 0.373
-
(2R)-4-hydroxy-3-oxo-3,4-dihydro-2H-1,4-benzoxazin-2-yl beta-D-glucopyranoside in 100 mM potassium phosphate buffer (pH 7.0), at 30°C Zea mays
2.1.1.241 additional information
-
additional information steady-state kinetic constants of BX7 Zea mays

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
1.14.11.59 cytoplasm
-
Zea mays 5737
-

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
2.1.1.241 additional information Mg2+ is not required for catalysis Zea mays

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
2.1.1.241 40000
-
x * 40000, native enzyme, SDS-PAGE Zea mays

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2.1.1.241 S-adenosyl-L-methionine + (2R)-4,7-dihydroxy-3-oxo-3,4-dihydro-2H-1,4-benzoxazin-2-yl beta-D-glucopyranoside Zea mays
-
S-adenosyl-L-homocysteine + (2R)-4-hydroxy-7-methoxy-3-oxo-3,4-dihydro-2H-1,4-benzoxazin-2-yl beta-D-glucopyranoside
-
?

Organism

EC Number Organism UniProt Comment Textmining
1.14.11.59 Zea mays
-
-
-
2.1.1.241 Zea mays
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
2.1.1.241 recombinant His-tagged enzyme from Escherichia coli by nickel affinity chromatography Zea mays

Source Tissue

EC Number Source Tissue Comment Organism Textmining
1.14.11.59 seedling highest expression Zea mays
-
2.1.1.241 seedling Bx7 is highest expressed in seedling tissue Zea mays
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.14.11.59 (2R)-4-hydroxy-3-oxo-3,4-dihydro-2H-1,4-benzoxazin-2-yl beta-D-glucopyranoside + 2-oxoglutarate + O2
-
Zea mays (2R)-4,7-dihydroxy-3-oxo-3,4-dihydro-2H-1,4-benzoxazin-2-yl beta-D-glucopyranoside + succinate + CO2 + H2O
-
?
1.14.11.59 additional information 2,4-dihydroxy-2H-1,4-benzoxazin-3(4H)-one is not hydroxylated by the enzyme Zea mays ?
-
?
2.1.1.241 additional information the only substance that serves as a substrate for the recombinant Bx7 is TRIBOA-Glc, neither the aglucone TRIBOA nor well-known substrates of plant O-methyltransferases are efficiently converted by the enzyme. In case of quercetin, a minor activity is detected. BX7 has no catalytic activity toward phenylpropanoids and flavonoids, e.g. apigenin is no substrate Zea mays ?
-
?
2.1.1.241 S-adenosyl-L-methionine + (2R)-4,7-dihydroxy-3-oxo-3,4-dihydro-2H-1,4-benzoxazin-2-yl beta-D-glucopyranoside
-
Zea mays S-adenosyl-L-homocysteine + (2R)-4-hydroxy-7-methoxy-3-oxo-3,4-dihydro-2H-1,4-benzoxazin-2-yl beta-D-glucopyranoside
-
?
2.1.1.241 S-adenosyl-L-methionine + (2R)-4,7-dihydroxy-3-oxo-3,4-dihydro-2H-1,4-benzoxazin-2-yl beta-D-glucopyranoside conversion of (2R)-2,4,7-trihydroxy-3-oxo-3,4-dihydro-2H-1,4-benzoxazin-2-yl beta-D-glucopyranoside, TRIBOA-Glc, to DIMBOA-Glc Zea mays S-adenosyl-L-homocysteine + (2R)-4-hydroxy-7-methoxy-3-oxo-3,4-dihydro-2H-1,4-benzoxazin-2-yl beta-D-glucopyranoside i.e. DIMBOA-Glc ?

Subunits

EC Number Subunits Comment Organism
2.1.1.241 ? x * 40000, native enzyme, SDS-PAGE Zea mays
2.1.1.241 More peptide mapping by mass spectrometry Zea mays

Synonyms

EC Number Synonyms Comment Organism
1.14.11.59 benzoxazinless6
-
Zea mays
1.14.11.59 BX6
-
Zea mays
1.14.11.59 DIBOA-Glc dioxygenase
-
Zea mays
2.1.1.241 BENZOXAZINLESS7
-
Zea mays
2.1.1.241 BX7
-
Zea mays
2.1.1.241 TRIBOA-OMT
-
Zea mays

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
1.14.11.59 2.1
-
(2R)-4-hydroxy-3-oxo-3,4-dihydro-2H-1,4-benzoxazin-2-yl beta-D-glucopyranoside in 100 mM potassium phosphate buffer (pH 7.0), at 30°C Zea mays

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
1.14.11.59 6
-
-
Zea mays

Cofactor

EC Number Cofactor Comment Organism Structure
2.1.1.241 S-adenosyl-L-methionine
-
Zea mays

General Information

EC Number General Information Comment Organism
2.1.1.241 metabolism Bx7 catalyzes the last step in benzoxazinoid biosynthesis of maize Zea mays
2.1.1.241 physiological function Bx7 is required for biosynthesis of the benzoxazinoid pesticide 2,4-dihydroxy-7-methoxy-2H-1,4-benzoxazin-3(4H)-one, i.e. DIMBOA, that is synthesized in seedlings and stored as glucoside in maize Zea mays

kcat/KM [mM/s]

EC Number kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
1.14.11.59 5.6
-
(2R)-4-hydroxy-3-oxo-3,4-dihydro-2H-1,4-benzoxazin-2-yl beta-D-glucopyranoside in 100 mM potassium phosphate buffer (pH 7.0), at 30°C Zea mays