Information on EC 1.10.3.15 - grixazone synthase

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The expected taxonomic range for this enzyme is: Streptomyces griseus

EC NUMBER
COMMENTARY hide
1.10.3.15
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RECOMMENDED NAME
GeneOntology No.
grixazone synthase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
2 3-amino-4-hydroxybenzoate + N-acetyl-L-cysteine + 2 O2 = grixazone B + 4 H2O + CO2
show the reaction diagram
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
grixazone biosynthesis
SYSTEMATIC NAME
IUBMB Comments
3-amino-4-hydroxybenzoate:N-acetyl-L-cysteine:oxygen oxidoreductase
A type 3 multi copper protein. The enzyme, isolated from the bacterium Streptomyces griseus, catalyses an 8 electron oxidation. Activation of the enzyme requires a copper chaperone (GriE). It also acts on 3-amino-4-hydroxybenzaldehyde, giving grixazone A. The second aldehyde group is presumably lost as formate. The enzyme also catalyses the reaction of EC 1.10.3.4 o-aminophenol oxidase.
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
metabolism
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
2-amino-4-methylphenol + N-acetyl-L-cysteine + O2
?
show the reaction diagram
-
-
-
-
?
2-amino-4-methylphenol + O2
?
show the reaction diagram
-
-
-
-
?
3,4-dihydroxybenzaldehyde + N-acetyl-L-cysteine + O2
?
show the reaction diagram
-
-
-
-
?
3,4-dihydroxybenzaldehyde + O2
?
show the reaction diagram
-
-
-
-
?
3-amino-4-hydroxybenzaldehyde + N-acetyl-L-cysteine + O2
grixazone A + H2O + CO2
show the reaction diagram
-
-
-
-
?
3-amino-4-hydroxybenzaldehyde + O2
?
show the reaction diagram
-
-
-
-
?
3-amino-4-hydroxybenzoate + N-acetyl-L-cysteine + O2
grixazone B + H2O + CO2
show the reaction diagram
4-amino-3-hydroxybenzoate + N-acetyl-L-cysteine + O2
?
show the reaction diagram
-
-
-
-
?
catechol + N-acetyl-L-cysteine + O2
?
show the reaction diagram
-
-
-
-
?
catechol + O2
?
show the reaction diagram
-
-
-
-
?
L-Dopa + N-acetyl-L-cysteine + O2
?
show the reaction diagram
-
-
-
-
?
o-aminophenol + N-acetyl-L-cysteine + O2
2-aminophenoxazin-3-one + H2O + CO2
show the reaction diagram
-
-
-
-
?
o-aminophenol + O2
?
show the reaction diagram
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-
-
-
?
protocatchuic acid + O2
?
show the reaction diagram
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-
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?
additional information
?
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the enzyme shows no monophenolase activity, although it oxidizes various o-aminophenols as preferable substrates rather than catechol-type substrates. The enzyme does not use tyrosine as a substrate
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NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
3-amino-4-hydroxybenzoate + N-acetyl-L-cysteine + O2
grixazone B + H2O + CO2
show the reaction diagram
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
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Zn2+, Ni2+, Co2+, Mn2+, Fe2+, or Mg2+ exert almost no effects
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2-Nitrophenol
3-amino-4-hydroxybenzensulfonic acid
4-hydroxy-3-nitrobenzaldehyde
4-hydroxybenzaldehyde
aniline
L-tyrosine
phenol
additional information
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10 mM EDTA and o-phenanthroline have negligible effects on the purified enzyme
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
GriE protein
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GriE activates the enzyme by transferring copper ions
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.75
2-amino-4-methylphenol
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at pH 7.0 and 55°C
0.41
3,4-Dihydroxybenzaldehyde
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at pH 7.0 and 55°C
0.58
3-amino-4-hydroxybenzaldehyde
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at pH 7.0 and 55°C
19
catechol
-
at pH 7.0 and 55°C
5.5
L-Dopa
-
at pH 7.0 and 55°C
3.5
o-aminophenol
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at pH 7.0 and 55°C
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
18
2-amino-4-methylphenol
Streptomyces griseus
-
at pH 7.0 and 55°C
0.8
3,4-Dihydroxybenzaldehyde
Streptomyces griseus
-
at pH 7.0 and 55°C
14
3-amino-4-hydroxybenzaldehyde
Streptomyces griseus
-
at pH 7.0 and 55°C
12
catechol
Streptomyces griseus
-
at pH 7.0 and 55°C
0.066
L-Dopa
Streptomyces griseus
-
at pH 7.0 and 55°C
20
o-aminophenol
Streptomyces griseus
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at pH 7.0 and 55°C
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
23
2-amino-4-methylphenol
Streptomyces griseus
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at pH 7.0 and 55°C
6922
0.97
3,4-Dihydroxybenzaldehyde
Streptomyces griseus
-
at pH 7.0 and 55°C
2458
24
3-amino-4-hydroxybenzaldehyde
Streptomyces griseus
-
at pH 7.0 and 55°C
11753
0.19
3-amino-4-hydroxybenzoate
Streptomyces griseus
-
at pH 7.0 and 55°C
12334
0.0073
4-Amino-3-hydroxybenzoate
Streptomyces griseus
-
at pH 7.0 and 55°C
29526
0.32
catechol
Streptomyces griseus
-
at pH 7.0 and 55°C
156
0.012
L-Dopa
Streptomyces griseus
-
at pH 7.0 and 55°C
320
5.8
o-aminophenol
Streptomyces griseus
-
at pH 7.0 and 55°C
4549
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
6.1
2-Nitrophenol
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at pH 7.0 and 55°C
31
3-amino-4-hydroxybenzensulfonic acid
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at pH 7.0 and 55°C
3.9
4-hydroxy-3-nitrobenzaldehyde
-
at pH 7.0 and 55°C
1.9
4-hydroxybenzaldehyde
-
at pH 7.0 and 55°C
14
aniline
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at pH 7.0 and 55°C
3.2
L-tyrosine
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at pH 7.0 and 55°C
21
phenol
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at pH 7.0 and 55°C
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.0000035
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crude extract, at pH 7.0 and 30°C
0.0658
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after 19000fold purification, at pH 7.0 and 30°C
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
8.5 - 10.5
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6 - 11
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more than 50% activity between pH 6.0 and 11.0
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
40 - 70
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more than 50% activity between 30 and 70°C
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
36000
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x * 36000, SDS-PAGE
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.5 - 8.5
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the enzyme is most stable at pH 6.5-8.5
674768
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
10 - 55
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when the enzyme sample is kept at pH 7.0 for 20 min, it remains active below 55°C, and activity drops sharply above 55°C
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Cu2+-charged HiTrap chelating column chromatography, HiTrap Q column chromatography, Resource PHE column chromatography, and Superdex 200 gel filtration
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli BL21(DE3)/pLysS cells
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