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Information on EC 1.13.11.5 - homogentisate 1,2-dioxygenase
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1.13.11.5 homogentisate 1,2-dioxygenaseIUBMB Comments
Requires Fe2+.
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Word Map
- 1.13.11.5
- alkaptonuria
-
ochronosis
- urine
- joint
- cartilage
- arthropathy
- sclera
- nitisinone
-
arthroplasty
-
discoloration
-
darken
- maleylacetoacetate
-
melanin-like
-
calculi
-
pyomelanin
-
ultra-rare
- 4-hydroxyphenylpyruvate
-
slovakia
- medicine
- ntbc
- diagnostics
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Synonyms
homogentisate 1,2-dioxygenase, homogentisic acid oxidase, homogentisate dioxygenase, homogentisate 1,2 dioxygenase, elhdo, homogentisic acid 1,2-dioxygenase, homogentisate oxidase, homogentisate oxygenase, homogentisate phytyl-transferase, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
EC 1.13.1.5
-
-
formerly
-
EC 1.99.2.5
-
-
formerly
-
HgD
HGDO
HGO
HGOa
HGOb
HmgA
homogentisate 1,2-dioxygenase
homogentisate dioxygenase
homogentisate oxidase
-
-
-
-
homogentisate oxygenase
-
-
-
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homogentisate phytyl-transferase
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involved in isoprenoid biosynthetic pathway
homogentisic acid oxidase
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-
-
-
homogentisic acid oxygenase
-
-
-
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homogentisic oxygenase
-
-
-
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homogentisicase
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-
-
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HTO
-
-
-
-
HGO
-
-
-
-
homogentisate dioxygenase
-
-
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
homogentisate + O2 = 4-maleylacetoacetate
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-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
oxidation
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-
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redox reaction
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-
-
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reduction
-
-
-
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PATHWAY SOURCE
PATHWAYS
BRENDA
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-
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SYSTEMATIC NAME
IUBMB Comments
homogentisate:oxygen 1,2-oxidoreductase (decyclizing)
Requires Fe2+.
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CAS REGISTRY NUMBER
COMMENTARY
9029-49-6
-
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
3-chlorohomogentisate + O2
3-chloro-4-maleylacetoacetate
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1% of activity with homogentisate
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-
?
3-methylhomogentisate + O2
3-methyl-4-maleylacetoacetate
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10% of activity with homogentisate
-
-
?
homogentisate + O2
4-fumarylacetoacetate
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homogentisic acid is oxidatively cleaved between carbons 1 and 2 to yield 4-fumarylacetoacetic acid, enzyme requires high oxygen tension for maximal activity
-
?
homogentisate + O2
4-maleylacetoacetate
Agave toumeyana
-
homogentisate ring-cleavage pathway, key enzyme of the ring-cleavage reaction in the catabolic sequence of enzymes from L-tyrosine to acetoacetate and fumarate
-
-
?
homogentisate + O2
4-maleylacetoacetate
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homogentisate ring-cleavage pathway, key enzyme of the ring-cleavage reaction in the catabolic sequence of enzymes from L-tyrosine to acetoacetate and fumarate
-
-
?
homogentisate + O2
4-maleylacetoacetate
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highly specific for homogentisate
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?
homogentisate + O2
4-maleylacetoacetate
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one of the enzymes mediating phenylalanine catabolism
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-
?
homogentisate + O2
4-maleylacetoacetate
catalyzes an essential step in phenylalanine catabolism
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-
?
homogentisate + O2
4-maleylacetoacetate
catalyzes an essential step in phenylalanine catabolism
-
-
?
homogentisate + O2
4-maleylacetoacetate
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specific for homogentisate
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?
homogentisate + O2
4-maleylacetoacetate
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one of the key enzymes involved in catabolism of phenylalanine, tyrosine, phenylacetic acid and hydroxyphenylacetic acids
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-
?
homogentisate + O2
4-maleylacetoacetate
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specific for homogentisate
-
?
homogentisate + O2
4-maleylacetoacetate
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one of the key enzymes involved in catabolism of phenylalanine, tyrosine, phenylacetic acid and hydroxyphenylacetic acids
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-
?
homogentisate + O2
4-maleylacetoacetate
Coleus scutellarioides
-
homogentisate ring-cleavage pathway, key enzyme of the ring-cleavage reaction in the catabolic sequence of enzymes from L-tyrosine to acetoacetate and fumarate
-
-
?
homogentisate + O2
4-maleylacetoacetate
-
homogentisate ring-cleavage pathway, key enzyme of the ring-cleavage reaction in the catabolic sequence of enzymes from L-tyrosine to acetoacetate and fumarate
-
-
?
homogentisate + O2
4-maleylacetoacetate
-
homogentisate ring-cleavage pathway, key enzyme of the ring-cleavage reaction in the catabolic sequence of enzymes from L-tyrosine to acetoacetate and fumarate
-
-
?
homogentisate + O2
4-maleylacetoacetate
ElHDO expression is induced during growth on ethylbenzene
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-
?
homogentisate + O2
4-maleylacetoacetate
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homogentisate ring-cleavage pathway, key enzyme of the ring-cleavage reaction in the catabolic sequence of enzymes from L-tyrosine to acetoacetate and fumarate
-
-
?
homogentisate + O2
4-maleylacetoacetate
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utilizes a nonheme iron to incorporate both atoms of molecular oxygen into homogentisate, identical with 2,5-dihydroxyphenylacetate
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?
homogentisate + O2
4-maleylacetoacetate
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enzyme catalyzes an intermediate step in the catabolism of tyrosine and phenylalanine
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-
?
homogentisate + O2
4-maleylacetoacetate
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enzyme cleaves the aromatic ring during the metabolic degradation of phenylalanine and tyrosine
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-
?
homogentisate + O2
4-maleylacetoacetate
-
homogentisate ring-cleavage pathway, key enzyme of the ring-cleavage reaction in the catabolic sequence of enzymes from L-tyrosine to acetoacetate and fumarate
-
-
?
homogentisate + O2
4-maleylacetoacetate
-
homogentisate is the natural substrate, key reaction in the catabolic pathway of aromatic amino acids, oxidative cleavage of the aromatic ring
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ir
homogentisate + O2
4-maleylacetoacetate
-
homogentisate ring-cleavage pathway, key enzyme of the ring-cleavage reaction in the catabolic sequence of enzymes from L-tyrosine to acetoacetate and fumarate
-
-
?
homogentisate + O2
4-maleylacetoacetate
-
homogentisate ring-cleavage pathway, key enzyme of the ring-cleavage reaction in the catabolic sequence of enzymes from L-tyrosine to acetoacetate and fumarate
-
-
?
homogentisate + O2
4-maleylacetoacetate
-
homogentisate ring-cleavage pathway, key enzyme of the ring-cleavage reaction in the catabolic sequence of enzymes from L-tyrosine to acetoacetate and fumarate
-
-
?
homogentisate + O2
4-maleylacetoacetate
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specific for homogentisate
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?
homogentisate + O2
4-maleylacetoacetate
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product is 4-maleylacetoacetate, which is converted by a specific cis-trans isomerase to 4-fumarylacetoacetate
?
homogentisate + O2
4-maleylacetoacetate
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homogentisate ring-cleavage pathway, key enzyme of the ring-cleavage reaction in the catabolic sequence of enzymes from L-tyrosine to acetoacetate and fumarate
-
-
?
homogentisate + O2
4-maleylacetoacetate
-
hmgA is necessary for tyrosine catabolism and the proper production of actinorhodin. Transcription of hmgA is activated by HpdA in the presence of tyrosine
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-
?
additional information
?
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not as substrates: phenylacetate, 2-hydroxyphenylacetate, 3-hydroxyphenylacetate, 4-hydroxyphenylacetate, phenylalanine, tyrosine, phenylpyruvate, gentisate
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-
?
additional information
?
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enzyme structure, conformation of the active site, enzyme contains a 280-residue N-terminal domain and a 140-residue C-terminal domain, associated as a hexamer arranged as a dimer of trimers
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-
?
additional information
?
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LB400 cells grown with 3-hydroxyphenylacetate degrade homogentisate and show homogentisate 1,2-dioxygenase, EC 1.13.11.5 activity
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-
?
additional information
?
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growth of the hmgA mutant on L-tyrosine as sole carbon and energy sources is impaired. Growth on L-tyrosine is restored and production of the brown melanin pigment is eliminated when the mutant is complemented with the wild-type hmgA gene. The change in aromatic amino acids metabolism caused by the deletion of the hmgA gene function does not impair production of phenazines and biological traits connected to these secondary compounds: inhibition of fungal growth and inhibition of barley seed germination
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-
?
additional information
?
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growth of the hmgA mutant on L-tyrosine as sole carbon and energy sources is impaired. Growth on L-tyrosine is restored and production of the brown melanin pigment is eliminated when the mutant is complemented with the wild-type hmgA gene. The change in aromatic amino acids metabolism caused by the deletion of the hmgA gene function does not impair production of phenazines and biological traits connected to these secondary compounds: inhibition of fungal growth and inhibition of barley seed germination
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-
?
additional information
?
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not as substrates: salicylic acid, catechol, 2,3-dihydroxybenzoic acid, 2,5-dihydroxybenzoic acid, 2,6-dihydroxybenzoic acid, o-hydroxyphenylacetic acid, p-hydroxyphenylacetic acid, 3,4-dihydroxyphenylacetic acid
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-
?
additional information
?
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-
enzyme contains essential sulfhydryl groups
-
-
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
homogentisate + O2
4-maleylacetoacetate
Agave toumeyana
-
homogentisate ring-cleavage pathway, key enzyme of the ring-cleavage reaction in the catabolic sequence of enzymes from L-tyrosine to acetoacetate and fumarate
-
-
?
homogentisate + O2
4-maleylacetoacetate
-
homogentisate ring-cleavage pathway, key enzyme of the ring-cleavage reaction in the catabolic sequence of enzymes from L-tyrosine to acetoacetate and fumarate
-
-
?
homogentisate + O2
4-maleylacetoacetate
-
one of the enzymes mediating phenylalanine catabolism
-
-
?
homogentisate + O2
4-maleylacetoacetate
catalyzes an essential step in phenylalanine catabolism
-
-
?
homogentisate + O2
4-maleylacetoacetate
catalyzes an essential step in phenylalanine catabolism
-
-
?
homogentisate + O2
4-maleylacetoacetate
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one of the key enzymes involved in catabolism of phenylalanine, tyrosine, phenylacetic acid and hydroxyphenylacetic acids
-
-
?
homogentisate + O2
4-maleylacetoacetate
-
one of the key enzymes involved in catabolism of phenylalanine, tyrosine, phenylacetic acid and hydroxyphenylacetic acids
-
-
?
homogentisate + O2
4-maleylacetoacetate
Coleus scutellarioides
-
homogentisate ring-cleavage pathway, key enzyme of the ring-cleavage reaction in the catabolic sequence of enzymes from L-tyrosine to acetoacetate and fumarate
-
-
?
homogentisate + O2
4-maleylacetoacetate
-
homogentisate ring-cleavage pathway, key enzyme of the ring-cleavage reaction in the catabolic sequence of enzymes from L-tyrosine to acetoacetate and fumarate
-
-
?
homogentisate + O2
4-maleylacetoacetate
-
homogentisate ring-cleavage pathway, key enzyme of the ring-cleavage reaction in the catabolic sequence of enzymes from L-tyrosine to acetoacetate and fumarate
-
-
?
homogentisate + O2
4-maleylacetoacetate
-
homogentisate ring-cleavage pathway, key enzyme of the ring-cleavage reaction in the catabolic sequence of enzymes from L-tyrosine to acetoacetate and fumarate
-
-
?
homogentisate + O2
4-maleylacetoacetate
-
enzyme catalyzes an intermediate step in the catabolism of tyrosine and phenylalanine
-
-
?
homogentisate + O2
4-maleylacetoacetate
-
enzyme cleaves the aromatic ring during the metabolic degradation of phenylalanine and tyrosine
-
-
?
homogentisate + O2
4-maleylacetoacetate
-
homogentisate ring-cleavage pathway, key enzyme of the ring-cleavage reaction in the catabolic sequence of enzymes from L-tyrosine to acetoacetate and fumarate
-
-
?
homogentisate + O2
4-maleylacetoacetate
-
homogentisate is the natural substrate, key reaction in the catabolic pathway of aromatic amino acids, oxidative cleavage of the aromatic ring
-
ir
homogentisate + O2
4-maleylacetoacetate
-
homogentisate ring-cleavage pathway, key enzyme of the ring-cleavage reaction in the catabolic sequence of enzymes from L-tyrosine to acetoacetate and fumarate
-
-
?
homogentisate + O2
4-maleylacetoacetate
-
homogentisate ring-cleavage pathway, key enzyme of the ring-cleavage reaction in the catabolic sequence of enzymes from L-tyrosine to acetoacetate and fumarate
-
-
?
homogentisate + O2
4-maleylacetoacetate
-
homogentisate ring-cleavage pathway, key enzyme of the ring-cleavage reaction in the catabolic sequence of enzymes from L-tyrosine to acetoacetate and fumarate
-
-
?
homogentisate + O2
4-maleylacetoacetate
-
homogentisate ring-cleavage pathway, key enzyme of the ring-cleavage reaction in the catabolic sequence of enzymes from L-tyrosine to acetoacetate and fumarate
-
-
?
homogentisate + O2
4-maleylacetoacetate
-
hmgA is necessary for tyrosine catabolism and the proper production of actinorhodin. Transcription of hmgA is activated by HpdA in the presence of tyrosine
-
-
?
additional information
?
-
-
LB400 cells grown with 3-hydroxyphenylacetate degrade homogentisate and show homogentisate 1,2-dioxygenase, EC 1.13.11.5 activity
-
-
?
additional information
?
-
-
growth of the hmgA mutant on L-tyrosine as sole carbon and energy sources is impaired. Growth on L-tyrosine is restored and production of the brown melanin pigment is eliminated when the mutant is complemented with the wild-type hmgA gene. The change in aromatic amino acids metabolism caused by the deletion of the hmgA gene function does not impair production of phenazines and biological traits connected to these secondary compounds: inhibition of fungal growth and inhibition of barley seed germination
-
-
?
additional information
?
-
-
growth of the hmgA mutant on L-tyrosine as sole carbon and energy sources is impaired. Growth on L-tyrosine is restored and production of the brown melanin pigment is eliminated when the mutant is complemented with the wild-type hmgA gene. The change in aromatic amino acids metabolism caused by the deletion of the hmgA gene function does not impair production of phenazines and biological traits connected to these secondary compounds: inhibition of fungal growth and inhibition of barley seed germination
-
-
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Fe2+
additional information
Fe2+
70% reduction of enzyme activity in crude extract in absence of Fe2+ and absolutely requirement for Fe2+ of the fusion protein of homogentisate dioxygenase and glutathione S-transferase, expressed in Escherichia coli
Fe2+
-
contains a nonheme Fe2+ at the active site, that is coordinated near the interface between subunits in the HGO trimer by Glu-341, His-335 and His-371
Fe2+
-
Fe2+ is an absolutely obligate cofactor and cannot be replaced by other divalent cations, highest enzyme activity in vitro at 2 mM Fe2+
Fe2+
required, ferrous ion content of 0.56 mol of iron per mol of protein, all twelve subunits in the a.u. contain fully occupied Fe sites, octahedral coordination for Fe2+ with two histidine residues (His331 and His367), the enzyme uses a mononuclear nonheme Fe2+ to catalyze the oxidative ring cleavage in the degradation of Tyr and Phe by producing maleylacetoacetate from homogentisate
Fe2+
-
contains non-porphyrin iron, valence change of enzymic iron during reaction: ferric and ferrous iron
additional information
-
other metallic ions, such as Fe3+, Co2+, Mn2+, Cu+ and Cu2+, cannot replace Fe2+
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
1,10-phenanthroline
-
inactivation in the absence of O2 due to formation of a white precipitate corresponding to apoprotein
2-hydroxyphenylacetate
-
strong competitive inhibition with respect to homogentisate
3-chlorohomogentisate
-
inactivation in the presence of O2 due to formation of a white precipitate corresponding to apoprotein
3-hydroxyphenylacetate
-
competitive inhibition with respect to homogentisate
Methylmercuric bromide
-
inhibits by competing with Fe2+ for a common enzymic binding site
p-hydroxyphenylacetic acid
-
80 mM, complete inhibition, substrate analogue
Superoxide dismutase
-
inhibits the reaction indicating the involvement of superoxide anions in the dioxygenase reaction
-
p-chloromercuribenzoate
-
inhibits by competing with Fe2+ for a common enzymic binding site
p-chloromercuribenzoate
-
competitive inhibition with respect to Fe2+ but not to homogentisate
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
ascorbate
-
dependent on the presence of ascorbate, presumably to maintain iron in the reduced form