Information on EC 4.1.99.20 - 3-amino-4-hydroxybenzoate synthase

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The expected taxonomic range for this enzyme is: Streptomyces griseus

EC NUMBER
COMMENTARY hide
4.1.99.20
-
RECOMMENDED NAME
GeneOntology No.
3-amino-4-hydroxybenzoate synthase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
2-amino-4,5-dihydroxy-6-oxo-7-(phosphonooxy)heptanoate = 3-amino-4-hydroxybenzoate + phosphate + 2 H2O
show the reaction diagram
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-
-
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
grixazone biosynthesis
SYSTEMATIC NAME
IUBMB Comments
2-amino-4,5-dihydroxy-6-oxo-7-(phosphonooxy)heptanoate hydro-lyase (cyclizing, 3-amino-4-hydroxybenzoate-forming)
Requires Mn2+ for maximum activity. The reaction is suggested to take place in several steps. Schiff base formation, double bond migration and dephosphorylation followed by ring opening and closing to form a pyrrolidine ring, and finally dehydration to form the product 3-amino-4-hydroxybenzoate. In the bacterium Streptomyces griseus the enzyme is involved in biosynthesis of grixazone, a yellow pigment that contains a phenoxazinone chromophore.
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
SwissProt
Manually annotated by BRENDA team
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-4,5-dihydroxy-6-oxo-7-(phosphonooxy)heptanoate
3-amino-4-hydroxybenzoate + phosphate + 2 H2O
show the reaction diagram
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
2-amino-4,5-dihydroxy-6-oxo-7-(phosphonooxy)heptanoate
3-amino-4-hydroxybenzoate + phosphate + 2 H2O
show the reaction diagram
A0JC76
the enzyme is involved in biosynthesis of grixazone, a yellow pigment that contains a phenoxazinone chromophore
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-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Co2+
0.1 mM, divalent mtal ion is essential for activity. Co2+ show 85% of the activity compared to Mn2+
Fe2+
0.1 mM, divalent mtal ion is essential for activity. Fe2+ show 81% of the activity compared to Mn2+
Mg2+
0.1 mM, divalent mtal ion is essential for activity. Mg2+ show 41% of the activity compared to Mn2+
Mn2+
0.1 mM, divalent mtal ion is essential for activity. Co2+, Fe2+ and Mg2+ can be used to a lesser extent than Mn2+
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
pyridoxal 5'-phosphate
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.012
2-amino-4,5-dihydroxy-6-oxo-7-(phosphonooxy)heptanoate
30°C, pH 7.2
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.025
2-amino-4,5-dihydroxy-6-oxo-7-(phosphonooxy)heptanoate
Streptomyces griseus
A0JC76
30°C, pH 7.2
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.5 - 9
pH 7.5: about 75% of maximal activity, pH 9.0: about 75% of maximal activity
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
46000
1 * 46000, SDS-PAGE
54000
gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
monomer
1 * 46000, SDS-PAGE
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.5 - 10.5
at 30°C, stable for 1 h
722650
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
30
at pH 7.2, 1 h, stable below
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli