Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 2.4.1.202 extracted from

  • Bailey, B.A.; Larson, R.L.
    Hydroxamic acid glucosyltransferases from maize seedlings (1989), Plant Physiol., 90, 1071-1076.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 2.4.1.202

Activating Compound

Activating Compound Comment Organism Structure
2-mercaptoethanol 5 mM, stimulation of 79% Zea mays
ascorbate at 5 mM, stimulation of 42% Zea mays
dithioerythritol 5 mM, stimulation of 96% Zea mays
glutathione 5 mM, stimulation of 92% Zea mays

Inhibitors

Inhibitors Comment Organism Structure
Cu2+ 5 mM, 3% remaining activity Zea mays
EDTA 16% decrease of activity Zea mays
Fe2+ 5 mM, 5% remaining activity Zea mays
N-ethylmaleimide at 1 mM, 96% decrease of activity, after addition of dithioerythritol, full activity Zea mays

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.174
-
 2,4-dihydroxy-7-methoxy-2H-1,4-benzoxazin-3(4H)-one enzyme in peak 2 Zea mays
0.217
-
 2,4-dihydroxy-7-methoxy-2H-1,4-benzoxazin-3(4H)-one enzyme in peak 1 Zea mays
0.28
-
 UDPglucose reaction with 2,4-dihydroxy-1,4-benzoxazin-3-one, enzyme in peak 2 Zea mays
0.286
-
 UDPglucose reaction with 2,4-dihydroxy-7-methoxy-2H-1,4-benzoxazin-3(4H)-one, enzyme in peak 1 Zea mays
0.638
-
 2,4-dihydroxy-1,4-benzoxazin-3-one enzyme in peak 2 Zea mays

Metals/Ions

Metals/Ions Comment Organism Structure
CaCl2 5 mM, stimulation Zea mays
MgCl2 5 mM, stimulation Zea mays

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
50000
-
 gel filtration, both peaks Zea mays

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
UDP-glucose + 2,4-dihydroxy-7-methoxy-2H-1,4-benzoxazin-3(4H)-one Zea mays
-
 UDP + 2,4-dihydroxy-7-methoxy-2H-1,4-benzoxazin-3(4H)-one 2-D-glucoside
-
 ?

Organism

Organism UniProt Comment Textmining
Zea mays
-
 two different enzymes with different substrate specificities, genes Bx8 and Bx9
-

Purification (Commentary)

Purification (Comment) Organism
partial, activity elutes from Q-Sepharose column in two peaks, named peak 1 and peak 2, exhibiting different activities towards substrates Zea mays

Source Tissue

Source Tissue Comment Organism Textmining
seedling
-
 Zea mays
-

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
1.218
-
 enzyme in peak 1 and peak 2 Zea mays

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
UDP-glucose + 2,4-dihydroxy-1,4-benzoxazin-3-one peak 1 glucosyltransferase has 3.6% of activity compared to activity towards 2,4-dihydroxy-7-methoxy-2H-1,4-benzoxazin-3(4H)-one, peak 2 glucosyltransferase has 57% of activity compared to activity towards 2,4-dihydroxy-7-methoxy-2H-1,4-benzoxazin-3(4H)-one Zea mays UDP + 2,4-dihydroxy-2H-1,4-benzoxazin-3-one 2-D-glucoside
-
 ?
UDP-glucose + 2,4-dihydroxy-7-methoxy-2H-1,4-benzoxazin-3(4H)-one
-
 Zea mays UDP + 2,4-dihydroxy-7-methoxy-2H-1,4-benzoxazin-3(4H)-one 2-D-glucoside
-
 ?

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
37
-
 assay at Zea mays
45
-
-
 Zea mays

Temperature Range [°C]

Temperature Minimum [°C] Temperature Maximum [°C] Comment Organism
25 55 88% of maximal activity at 55°C, 60% of maximal activity at 25°C Zea mays

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
8.5
-
-
 Zea mays

pH Range

pH Minimum pH Maximum Comment Organism
6.5 10 10% of maximal activity at pH 6.5 and 30% of maximal activity at pH 10.0 Zea mays

Cofactor

Cofactor Comment Organism Structure
ascorbate at 5 mM, stimulation of 42% Zea mays