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3-chlorohomogentisate + O2
3-chloro-4-maleylacetoacetate
-
1% of activity with homogentisate
-
-
?
3-methylhomogentisate + O2
3-methyl-4-maleylacetoacetate
-
10% of activity with homogentisate
-
-
?
homogentisate + O2
4-fumarylacetoacetate
homogentisate + O2
4-maleylacetoacetate
additional information
?
-
homogentisate + O2
4-fumarylacetoacetate
-
-
-
?
homogentisate + O2
4-fumarylacetoacetate
-
-
-
?
homogentisate + O2
4-fumarylacetoacetate
Pigeon
-
-
-
?
homogentisate + O2
4-fumarylacetoacetate
-
-
-
?
homogentisate + O2
4-fumarylacetoacetate
-
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 + 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 + 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
-
-
-
ir
homogentisate + O2
4-maleylacetoacetate
-
-
?
homogentisate + O2
4-maleylacetoacetate
-
highly specific for homogentisate
-
?
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
-
-
?
homogentisate + O2
4-maleylacetoacetate
catalyzes an essential step in phenylalanine catabolism
-
-
?
homogentisate + O2
4-maleylacetoacetate
-
specific for homogentisate
-
?
homogentisate + O2
4-maleylacetoacetate
-
one of the key enzymes involved in catabolism of phenylalanine, tyrosine, phenylacetic acid and hydroxyphenylacetic acids
-
-
?
homogentisate + O2
4-maleylacetoacetate
-
specific for homogentisate
-
?
homogentisate + O2
4-maleylacetoacetate
-
one of the key enzymes involved in catabolism of phenylalanine, tyrosine, phenylacetic acid and hydroxyphenylacetic acids
-
-
?
homogentisate + O2
4-maleylacetoacetate
-
-
-
-
?
homogentisate + O2
4-maleylacetoacetate
-
-
-
-
?
homogentisate + O2
4-maleylacetoacetate
Coleus scutellarioides
-
-
-
?
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 + 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 + 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
-
-
?
homogentisate + O2
4-maleylacetoacetate
-
-
-
?
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 + O2
4-maleylacetoacetate
-
-
-
-
?
homogentisate + O2
4-maleylacetoacetate
-
-
?
homogentisate + O2
4-maleylacetoacetate
-
-
-
?
homogentisate + O2
4-maleylacetoacetate
-
-
-
-
?
homogentisate + O2
4-maleylacetoacetate
-
-
-
?
homogentisate + O2
4-maleylacetoacetate
-
-
-
ir
homogentisate + O2
4-maleylacetoacetate
-
utilizes a nonheme iron to incorporate both atoms of molecular oxygen into homogentisate, identical with 2,5-dihydroxyphenylacetate
-
?
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 + 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 + O2
4-maleylacetoacetate
-
-
-
?
homogentisate + O2
4-maleylacetoacetate
-
-
-
?
homogentisate + O2
4-maleylacetoacetate
-
-
-
-
?
homogentisate + O2
4-maleylacetoacetate
-
-
-
ir
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 catabolism
-
-
?
homogentisate + O2
4-maleylacetoacetate
-
-
-
?
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 + O2
4-maleylacetoacetate
-
-
-
-
?
homogentisate + O2
4-maleylacetoacetate
-
-
-
-
?
homogentisate + O2
4-maleylacetoacetate
-
-
-
-
?
homogentisate + O2
4-maleylacetoacetate
-
-
-
-
ir
homogentisate + O2
4-maleylacetoacetate
-
-
-
?
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 + 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 + O2
4-maleylacetoacetate
-
specific for homogentisate
-
?
homogentisate + O2
4-maleylacetoacetate
-
-
-
-
ir
homogentisate + O2
4-maleylacetoacetate
-
-
-
?
homogentisate + O2
4-maleylacetoacetate
-
-
-
?
homogentisate + O2
4-maleylacetoacetate
-
-
-
-
ir
homogentisate + O2
4-maleylacetoacetate
-
-
product is 4-maleylacetoacetate, which is converted by a specific cis-trans isomerase to 4-fumarylacetoacetate
?
homogentisate + O2
4-maleylacetoacetate
-
-
-
?
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
?
-
gentisate is not a substrate
-
-
?
additional information
?
-
-
gentisate is not a substrate
-
-
?
additional information
?
-
-
not as substrates: phenylacetate, 2-hydroxyphenylacetate, 3-hydroxyphenylacetate, 4-hydroxyphenylacetate, phenylalanine, tyrosine, phenylpyruvate, gentisate
-
-
?
additional information
?
-
-
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
-
-
?
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
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
-
enzyme contains essential sulfhydryl groups
-
-
?
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metabolism
-
the enzyme is involved in tyrosine catabolism
evolution
-
the G161R natural mutation in the HGD gene occurs in a Hungarian population, originating from Slovakia, resists over 300 years, alkaptonuria phenotype overview
evolution
despite different folds, active site architectures, and Fe2+ coordination, extradiol dioxygenases can proceed through the same principal reaction intermediatesto catalyze the O2-dependent cleavage of aromatic rings. Convergent evolution of nonhomologous enzymes using the 2-His-1-carboxylate facial triad motif developed different solutions to stabilize closely related intermediates in unlike environments
evolution
-
despite different folds, active site architectures, and Fe2+ coordination, extradiol dioxygenases can proceed through the same principal reaction intermediatesto catalyze the O2-dependent cleavage of aromatic rings. Convergent evolution of nonhomologous enzymes using the 2-His-1-carboxylate facial triad motif developed different solutions to stabilize closely related intermediates in unlike environments
-
malfunction
-
alkaptonuria is a rare autosomal recessive disease, associated with deficiency of homogentisate 1,2-dioxygenase activity in the liver. This leads to an accumulation of homogentisic acid and its oxidized derivatives in polymerized form in connective tissues, especially in joints. Homogentisic acid induces apoptosis in chondrocytes. N-acetylcysteine decreases apoptosis induced in chondrocytes by HGA, increases chondrocyte growth reduced by homogentisate, and partially restores proteoglycan release inhibited by homogentisate, the effect is improved by addition of ascorbic acid. Evaluation of antioxidant drugs for the treatment of ochronotic alkaptonuria, caused by homogentisate 1,2-dioxygenase activity mutation, in an in vitro human cell model, overview
malfunction
alkaptonuria results from defective homogentisate1,2-dioxygenase, causing degenerative arthropathy. The deposition of ochronotic pigment in joints is so far attributed to homogentisic acid produced by the liver, circulating in the blood and accumulating locally. Alkaptonuria osteoarticular cells produce the ochronotic pigment in loco and this may strongly contribute to induction of ochronotic arthropath
malfunction
enzyme mutations in the homogentisate 1,2 dioxygenase gene are responsible for alkaptonuria in patients among Jordanian population, genotyping, overview
malfunction
Alkaptonuria (AKU) is an ultra-rare disease caused by mutations in homogentisate 1,2-dioxygenase (HGD) enzyme, characterized by the loss of enzymatic activity and the accumulation of its substrate, homogentisic acid (HGA) in different tissues, leading to ochronosis and organ degeneration
malfunction
alkaptonuria is an autosomal recessive disorder, which is caused by a site-specific mutation(s) and thus, impairs the function of homogentisate-1, 2-dioxygenase
malfunction
alkaptonuria is an autosomal recessive disorder, which is caused by a site-specific mutations and thus, impairs the function of homogentisate-1,2-dioxygenase
malfunction
alkaptonuria is an inherited disease caused by homogentisate 1,2-dioxygenase deficiency
malfunction
alkaptonuria is an inherited disease that is caused by homogenticate accumulation. Deficiency or mutation in homogentisate 1,2-dioxygenase gene (chromosome 3q21-q23) lead to production of incorrectly folded or truncated enzyme
malfunction
alkaptonuria is caused by homogentisate 1,2-dioxygenase deficiency. Homogentisate 1,2-dioxygenase deficiency in the liver is responsible for homogentisic acid derived ochronotic pigmentation
malfunction
ADH05034.1
disruption of the hmgA gene encoding homogentisate dioxygenase in BMB171 induces the accumulation of the homogentisic acid and provokes an increased pigment (pyomelanin) formation
malfunction
-
disruption of the hmgA gene encoding homogentisate dioxygenase in BMB171 induces the accumulation of the homogentisic acid and provokes an increased pigment (pyomelanin) formation
-
physiological function
Vitis vinifera x Vitis vinifera
-
involved in aromatic amino acid metabolism
physiological function
-
involved in aromatic amino acid metabolism
physiological function
homogentisate 1,2-dioxygenase uses a mononuclear nonheme Fe2+ to catalyze the oxidative ring cleavage in the degradation of Tyr and Phe by producing maleylacetoacetate from homogentisate, i.e 2,5-dihydroxyphenylacetate
physiological function
-
homogentisate 1,2-dioxygenase is a potentially critical enzyme for regulation of pigment production
physiological function
essential enzyme for the catabolism of phenylalanine and tyrosine
physiological function
-
homogentisate 1,2-dioxygenase is a potentially critical enzyme for regulation of pigment production
-
physiological function
-
homogentisate 1,2-dioxygenase uses a mononuclear nonheme Fe2+ to catalyze the oxidative ring cleavage in the degradation of Tyr and Phe by producing maleylacetoacetate from homogentisate, i.e 2,5-dihydroxyphenylacetate
-
additional information
HGD-BstXI genotypes show significant effects on cooking loss, drip loss, net meat weight, carcass weight, and eye muscle area. Also the HGD-HaeIII genotypes significantly affect cooking loss, muscle fibre diameter, shear force, drip loss, and carcass yield ratio. Phenotypes, overview
additional information
-
mutations in homogentisate 1,2-dioxygenase cause alkaptonuria and subsequent ochronosis, an uncommon cause of backache. The phenotype includes limited spine mobility and chronic disk degeneration, overview
additional information
the active site pocket with its Fe2+ ion is freely accessible from the outside through a wide opening. Homogentisate binds as a monodentate ligand to Fe2+, and its interaction with Tyr346 invokes the folding of a loop over the active site, effectively shielding it from solvent. Binding of homogentisate is driven by enthalpy and is entropically disfavored as shown by anoxic isothermal titration calorimetry. Three different reaction cycle intermediates, i.e. superoxo:semiquinone-, alkylperoxo-, and product-bound intermediates. central role of Y346 in substrate binding and turnover
additional information
-
the active site pocket with its Fe2+ ion is freely accessible from the outside through a wide opening. Homogentisate binds as a monodentate ligand to Fe2+, and its interaction with Tyr346 invokes the folding of a loop over the active site, effectively shielding it from solvent. Binding of homogentisate is driven by enthalpy and is entropically disfavored as shown by anoxic isothermal titration calorimetry. Three different reaction cycle intermediates, i.e. superoxo:semiquinone-, alkylperoxo-, and product-bound intermediates. central role of Y346 in substrate binding and turnover
-
additional information
-
HGD-BstXI genotypes show significant effects on cooking loss, drip loss, net meat weight, carcass weight, and eye muscle area. Also the HGD-HaeIII genotypes significantly affect cooking loss, muscle fibre diameter, shear force, drip loss, and carcass yield ratio. Phenotypes, overview
-
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D120A
ADH05034.1
transformant shows a non-pigmented phenotype
F136A
ADH05034.1
transformant shows a pigmented phenotype
G119A
ADH05034.1
transformant shows a non-pigmented phenotype
G128A
ADH05034.1
transformant shows a pigmented phenotype
G241A
ADH05034.1
transformant shows a pigmented phenotype
G272E
ADH05034.1
mutation is responsible for pigment overproduction in Bacillus thuringiensis BMB181
G323A
ADH05034.1
transformant shows a non-pigmented phenotype
G89A
ADH05034.1
transformant shows a non-pigmented phenotype
H261A
ADH05034.1
transformant shows a pigmented phenotype
H334A
ADH05034.1
transformant shows a pigmented phenotype
K219A
ADH05034.1
transformant shows a non-pigmented phenotype
N116A
ADH05034.1
transformant shows a non-pigmented phenotype
N300A
ADH05034.1
transformant shows a non-pigmented phenotype
P245A
ADH05034.1
transformant shows a non-pigmented phenotype
P336A
ADH05034.1
transformant shows a pigmented phenotype
D120A
-
transformant shows a non-pigmented phenotype
-
F136A
-
transformant shows a pigmented phenotype
-
H261A
-
transformant shows a pigmented phenotype
-
H334A
-
transformant shows a pigmented phenotype
-
N300A
-
transformant shows a non-pigmented phenotype
-
C1273A
naturally occuring mutation, the mutation is involved in alkaptonuria
E401Q
the missense variant E401Q is responsible for development of Alkaptonuria
E42A
the mutant shows strongly reduced specific activity compared to the wild type enzyme
G161R
-
naturally occuring mutation in the HGD gene, resulting in a specific genotype appearing in a Hungarian population, originating from Slovakia, with alkaptonuria, phenotype overview
G360R
active site mutation in exon 13
H80Q
the mutant shows slightly reduced specific activity compared to the wild type enzyme
I216T
the mutant shows strongly reduced specific activity compared to the wild type enzyme
K57N
active site mutation in exon 3
M368V
the mutant shows strongly reduced specific activity compared to the wild type enzyme
R225H
the mutant shows strongly reduced specific activity compared to the wild type enzyme
S189I
the mutant shows strongly reduced specific activity compared to the wild type enzyme
T1046G
naturally occuring mutation, the mutation is involved in alkaptonuria
T533G
naturally occuring mutation, the mutation is involved in alkaptonuria
T847C
naturally occuring mutation, the mutation is involved in alkaptonuria
Y62C
the mutant shows strongly reduced specific activity compared to the wild type enzyme
H288Q
site-directed mutagenesis, the mutant shows a 75fold reduction in kcat compared to the wild-type enzyme
Y346F
site-directed mutagenesis, replacement of Y346 by phenylalanine decreases the affinity for homogentisate more than 60fold and reduces the apparent kcat 20fold resulting in a decrease of the specificity constant by three orders of magnitude compared to the wild-type enzyme
H288Q
-
site-directed mutagenesis, the mutant shows a 75fold reduction in kcat compared to the wild-type enzyme
-
Y346F
-
site-directed mutagenesis, replacement of Y346 by phenylalanine decreases the affinity for homogentisate more than 60fold and reduces the apparent kcat 20fold resulting in a decrease of the specificity constant by three orders of magnitude compared to the wild-type enzyme
-
R378G
-
the mutation is associated with the loss of pigmentation
R378G
-
the mutation is associated with the loss of pigmentation
-
A122D
the mutant shows strongly reduced specific activity compared to the wild type enzyme
A122D
loss of structural and molecular dynamic properties of the enzyme, the mutation is potentially related with the severity of alkaptonuria
A122D
the mutation is potentially related with the severity of alkaptonuria
V300G
loss of structural and molecular dynamic properties of the enzyme, the mutation is potentially related with the severity of alkaptonuria
V300G
the mutation is potentially related with the severity of alkaptonuria
W60G
the mutant shows strongly reduced specific activity compared to the wild type enzyme
W60G
loss of structural and molecular dynamic properties of the enzyme, the mutation is potentially related with the severity of alkaptonuria
W60G
the mutation is potentially related with the severity of alkaptonuria
additional information
-
strain carrying an homogentisate dioxygenase gene disruption with full genotype biA1, methG1, deltahmgA without enzyme activity
additional information
mutant strain biA1, methG1, argB2 with homogentisate dioxygenase gene disruption has no homogentisate dioxygenase activity and accumulates homogentisate
additional information
-
mutant strain biA1, methG1, argB2 with homogentisate dioxygenase gene disruption has no homogentisate dioxygenase activity and accumulates homogentisate
additional information
-
mutant strain biA1, methG1, argB2 with homogentisate dioxygenase gene disruption has no homogentisate dioxygenase activity and accumulates homogentisate
-
additional information
-
human gene for alkaptonuria is mapped to chromosome 3q2
additional information
alkaptonuric humans are deficient for homogentisate 1,2-dioxygenase and carry two copies of a loss-of-function allele of HGO gene
additional information
-
alkaptonuric humans are deficient for homogentisate 1,2-dioxygenase and carry two copies of a loss-of-function allele of HGO gene
additional information
-
20 missence mutations in HGO from alkaptonuria patients
additional information
the 551-552insG mutation is involved in alkaptonuria
additional information
-
the 551-552insG mutation is involved in alkaptonuria
additional information
-
-
additional information
-
alkaptonuric mouse lacks enzyme activity and have recessive mutation aku, mapped to chromosome 16, inbred strain C57BLG/J is heterozygous for the aku mutation
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Nozaki, M.
Nonheme iron dioxygenase
Mol. Mech. Oxygen Activ. (Hayaishi, O., ed.) Academic Press, New York
135-165
1974
Bos taurus, Pseudomonas fluorescens
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brenda
Adachi, K.; Iwayama, Y.; Tanioka, H.; Takeda, Y.
Purification and properties of homogentisate oxygenase from Pseudomonas fluorescens
Biochim. Biophys. Acta
118
88-97
1966
Pseudomonas fluorescens
brenda
Ravdin, R.G.; Crandall, D.I.
The enzymatic conversion of homogentisic acid to 4-fumarylacetoacetic acid
J. Biol. Chem.
189
137-149
1951
Rattus norvegicus
brenda
Knox, W.E.; Edwards, S.W.
Homogentisate oxidase of liver
J. Biol. Chem.
216
479-487
1955
Rattus norvegicus
brenda
Crandall, D.I.; Halikis, D.N.
Homogentisic acid oxidase. I. Distribution in animal tissues and relation to tyrosine metabolism in rat kidney
J. Biol. Chem.
208
629-638
1954
Cavia porcellus, Oryctolagus cuniculus, Pigeon, Rattus norvegicus
brenda
Durand, R.; Zenk, M.H.
Enzymes of the homogentisate ring-cleavage pathway in cell suspension cultures of higher plants
FEBS Lett.
39
218-220
1974
Agave toumeyana, Agrostemma githago, Coleus scutellarioides, Daucus carota, Drosophyllum lusitanicum, Glycine max, Melilotus albus, Nicotiana sylvestris, Phaseolus vulgaris, Pimpinella anisum, Ruta graveolens
brenda
Sugumaran, M.; Vaidyanathan, C.S.
Affinity chromatography of homogentisate-1,2-dioxygenase from Aspergillus niger
FEMS Microbiol. Lett.
4
343-347
1978
Aspergillus niger, Aspergillus niger UBC 814
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brenda
Granadino, B.; Beltran-Valero de Bernabe, D.; Fernandez-Canon, J.M.; Penalva, M.A.; Rodriguez de Cordoba, S.
The human homogentisate 1,2-dioxygenase (HGO) gene
Genomics
43
115-122
1997
Homo sapiens (Q93099), Homo sapiens
brenda
Schmidt, S.R.; Gehrig, A.; Koehler, M.R.; Schmid, M.; Muller, C.R.; Kress, W.
Cloning of the homogentisate 1,2-dioxygenase gene, the key enzyme of alkaptonuria in mouse
Mamm. Genome
8
168-171
1997
Mus musculus
brenda
Fernandez-Canon, J.M.; Penalva, M.A.
Spectrophotometric determination of homogentisate using Aspergillus nidulans homogentisate dioxygenase
Anal. Biochem.
245
218-221
1997
Aspergillus nidulans
brenda
Hudecova, S.; Strakova, Z.; Krizanova, O.
Purification of the homogentisic acid oxidase from mammalian liver
Int. J. Biochem. Cell Biol.
27
1357-1363
1995
Bos taurus, Oryctolagus cuniculus, Homo sapiens, Mus musculus
brenda
Fernandez-Canon, J.M.; Penalva, M.A.
Molecular characterization of a gene encoding a homogentisate dioxygenase from Aspergillus nidulans and identification of its human and plant homologues
J. Biol. Chem.
270
21199-21205
1995
Aspergillus nidulans (Q00667), Aspergillus nidulans, Aspergillus nidulans BiA1 (Q00667)
brenda
Titus, G.P.; Mueller, H.A.; Burgner, J.; Rodriguez de Cordoba, S.; Penalva, M.A.; Timm, D.E.
Crystal structure of human homogentisate dioxygenase
Nat. Struct. Biol.
7
542-546
2000
Bos taurus, Homo sapiens, Mus musculus
brenda
Schmidt, S.R.; Muller, C.R.; Kress, W.
Murine liver homogentisate 1,2-dioxygenase. Purification to homogeneity and novel biochemical properties
Eur. J. Biochem.
228
425-430
1995
Mus musculus
brenda
Gunsch, C.K.; Cheng, Q.; Kinney, K.A.; Szaniszlo, P.J.; Whitman, C.P.
Identification of a homogentisate-1,2-dioxygenase gene in the fungus Exophiala lecanii-corni: analysis and implications
Appl. Microbiol. Biotechnol.
68
405-411
2005
Exophiala lecanii-corni (Q6JDV6), Exophiala lecanii-corni
brenda
Veldhuizen, E.J.; Vaillancourt, F.H.; Whiting, C.J.; Hsiao, M.M.; Gingras, G.; Xiao, Y.; Tanguay, R.M.; Boukouvalas, J.; Eltis, L.D.
Steady-state kinetics and inhibition of anaerobically purified human homogentisate 1,2-dioxygenase
Biochem. J.
386
305-314
2005
Homo sapiens
brenda
Dixon, D.P.; Edwards, R.
Enzymes of tyrosine catabolism in Arabidopsis thaliana
Plant Sci.
171
360-366
2006
Arabidopsis thaliana (Q9ZRA2), Arabidopsis thaliana
brenda
Shimizu, M.; Yuda, N.; Nakamura, T.; Tanaka, H.; Wariishi, H.
Metabolic regulation at the tricarboxylic acid and glyoxylate cycles of the lignin-degrading basidiomycete Phanerochaete chrysosporium against exogenous addition of vanillin
Proteomics
5
3919-3931
2005
Phanerodontia chrysosporium
brenda
Borowski, T.; Georgiev, V.; Siegbahn, P.E.
Catalytic reaction mechanism of homogentisate dioxygenase: a hybrid DFT study
J. Am. Chem. Soc.
127
17303-17314
2005
Homo sapiens (Q93099), Homo sapiens
brenda
Kim, Y.H.; Cho, K.; Yun, S.H.; Kim, J.Y.; Kwon, K.H.; Yoo, J.S.; Kim, S.I.
Analysis of aromatic catabolic pathways in Pseudomonas putida KT 2440 using a combined proteomic approach: 2-DE/MS and cleavable isotope-coded affinity tag analysis
Proteomics
6
1301-1318
2006
Pseudomonas putida, Pseudomonas putida KT 2440
brenda
Kang, B.R.; Han, S.H.; Cho, S.M.; Anderson, A.J.; Kim, I.S.; Park, S.K.; Kim, Y.C.
Characterization of a homogentisate dioxygenase mutant in Pseudomonas chlororaphis O6
Curr. Microbiol.
56
145-149
2008
Pseudomonas chlororaphis, Pseudomonas chlororaphis O6
brenda
Yoon, S.S.; Karabulut, A.C.; Lipscomb, J.D.; Hennigan, R.F.; Lymar, S.V.; Groce, S.L.; Herr, A.B.; Howell, M.L.; Kiley, P.J.; Schurr, M.J.; Gaston, B.; Choi, K.H.; Schweizer, H.P.; Hassett, D.J.
Two-pronged survival strategy for the major cystic fibrosis pathogen, Pseudomonas aeruginosa, lacking the capacity to degrade nitric oxide during anaerobic respiration
EMBO J.
26
3662-3672
2007
Pseudomonas aeruginosa
brenda
Zhang, Y.; Wang, L.; Zhang, S.; Yang, H.; Tan, H.
hmgA, transcriptionally activated by HpdA, influences the biosynthesis of actinorhodin in Streptomyces coelicolor
FEMS Microbiol. Lett.
280
219-225
2008
Streptomyces coelicolor
brenda
Grasko, J.M.; Hooper, A.J.; Brown, J.W.; McKnight, C.J.; Burnett, J.R.
A novel missense HGD gene mutation, K57N, in a patient with alkaptonuria
Clin. Chim. Acta
403
254-256
2009
Homo sapiens (Q93099)
brenda
Munne-Bosch, S.; Falara, V.; Pateraki, I.; Lopez-Carbonell, M.; Cela, J.; Kanellis, A.K.
Physiological and molecular responses of the isoprenoid biosynthetic pathway in a drought-resistant Mediterranean shrub, Cistus creticus exposed to water deficit
J. Plant Physiol.
166
136-145
2009
Cistus creticus
brenda
Battilana, J.; Costantini, L.; Emanuelli, F.; Sevini, F.; Segala, C.; Moser, S.; Velasco, R.; Versini, G.; Stella Grando, M.
The 1-deoxy-D: -xylulose 5-phosphate synthase gene co-localizes with a major QTL affecting monoterpene content in grapevine
Theor. Appl. Genet.
118
653-669
2009
Vitis vinifera x Vitis vinifera, Vitis vinifera x Vitis riparia
brenda
Tinti, L.; Spreafico, A.; Braconi, D.; Millucci, L.; Bernardini, G.; Chellini, F.; Cavallo, G.; Selvi, E.; Galeazzi, M.; Marcolongo, R.; Gallagher, J.A.; Santucci, A.
Evaluation of antioxidant drugs for the treatment of ochronotic alkaptonuria in an in vitro human cell model
J. Cell. Physiol.
225
84-91
2010
Homo sapiens
brenda
Toth, K.; Kiss-Laaszlo, Z.; Lenart, E.; Juhasz, K.; Takacs, K.; Bender, T.; Szabo, J.
Familiar ochronotic arthropathy-caused by a gene mutation traced three hundred years
Joint Bone Spine
77
355-357
2010
Homo sapiens
brenda
Zhou, G.L.; Cao, Y.; Li, M.; Zhang, L.C.; Yu, Y.S.; Jin, H.G.
Meat quality and carcass traits in relation to HGD-BstXI and HGD-HaeIII PCR-RFLP polymorphism in Chinese red cattle
Meat Sci.
85
270-273
2010
Bos taurus (B8YB76), Bos taurus Chinese red cattle (B8YB76)
brenda
Effelsberg, N.; Huegle, T.; Walker, U.
A metabolic cause of spinal deformity
Metab. Clin. Exp.
59
140-143
2010
Homo sapiens
brenda
Zhou, G.; Dudgeon, C.; Li, M.; Cao, Y.; Zhang, L.; Jin, H.
Molecular cloning of the HGD gene and association of SNPs with meat quality traits in Chinese red cattle
Mol. Biol. Rep.
37
603-611
2010
Bos taurus (B8YB76)
brenda
Laschi, M.; Tinti, L.; Braconi, D.; Millucci, L.; Ghezzi, L.; Amato, L.; Selvi, E.; Spreafico, A.; Bernardini, G.; Santucci, A.
Homogentisate 1,2 dioxygenase is expressed in human osteoarticular cells: implications in alkaptonuria
J. Cell. Physiol.
227
3254-3257
2012
Homo sapiens (Q93099), Homo sapiens
brenda
Mendez, V.; Agullo, L.; Gonzalez, M.; Seeger, M.
The homogentisate and homoprotocatechuate central pathways are involved in 3- and 4-hydroxyphenylacetate degradation by Burkholderia xenovorans LB400
PLoS ONE
6
e17583
2011
Paraburkholderia xenovorans
brenda
Jeoung, J.H.; Bommer, M.; Lin, T.Y.; Dobbek, H.
Visualizing the substrate-, superoxo-, alkylperoxo-, and product-bound states at the nonheme Fe(II) site of homogentisate dioxygenase
Proc. Natl. Acad. Sci. USA
110
12625-12630
2013
Pseudomonas putida (Q88E47), Pseudomonas putida KT 2240 (Q88E47)
brenda
Al-sbou, M.
Novel mutations in the homogentisate 1,2 dioxygenase gene identified in Jordanian patients with alkaptonuria
Rheumatol. Int.
32
1741-1746
2012
Homo sapiens (Q93099), Homo sapiens
brenda
Bernini, A.; Galderisi, S.; Spiga, O.; Bernardini, G.; Niccolai, N.; Manetti, F.; Santucci, A.
Toward a generalized computational workflow for exploiting transient pockets as new targets for small molecule stabilizers Application to the homogentisate 1,2-dioxygenase mutants at the base of rare disease alkaptonuria
Comput. Biol. Chem.
70
133-141
2017
Homo sapiens (Q93099)
brenda
Mori, T.; Koyama, G.; Kawagishi, H.; Hirai, H.
Effects of homologous expression of 1,4-benzoquinone reductase and homogentisate 1,2-dioxygenase genes on wood decay in hyper-lignin-degrading fungus Phanerochaete sordida YK-624
Curr. Microbiol.
73
512-518
2016
Phanerochaete sordida, Phanerochaete sordida YK-624
brenda
Gonyar, L.A.; Fankhauser, S.C.; Goldberg, J.B.
Single amino acid substitution in homogentisate 1,2-dioxygenase is responsible for pigmentation in a subset of Burkholderia cepacia complex isolates
Environ. Microbiol. Rep.
7
180-187
2015
Burkholderia cepacia, Burkholderia cepacia K56-2
brenda
Bernardini, G.; Laschi, M.; Geminiani, M.; Braconi, D.; Vannuccini, E.; Lupetti, P.; Manetti, F.; Millucci, L.; Santucci, A.
Homogentisate 1,2 dioxygenase is expressed in brain implications in alkaptonuria
J. Inherit. Metab. Dis.
38
807-814
2015
Homo sapiens, Mus musculus
brenda
Zolfaghari, N.
Molecular docking analysis of nitisinone with homogentisate 1,2 dioxygenase
Bioinformation
13
136-139
2017
Homo sapiens (Q93099)
brenda
Bernini, A.; Galderisi, S.; Spiga, O.; Amarabom, C.O.; Santucci, A.
Transient pockets as mediators of gas molecules routes inside proteins The case study of dioxygen pathway in homogentisate 1,2-dioxygenase and its implication in Alkaptonuria development
Comput. Biol. Chem.
88
107356
2020
Homo sapiens (Q93099)
brenda
Yang, W.; Ruan, L.; Tao, J.; Peng, D.; Zheng, J.; Sun, M.
Single amino acid substitution in homogentisate dioxygenase affects melanin production in Bacillus thuringiensis
Front. Microbiol.
9
2242
2018
Bacillus thuringiensis (ADH05034.1), Bacillus thuringiensis, Bacillus thuringiensis BMB171 (ADH05034.1)
brenda
Hughes, J.H.; Liu, K.; Plagge, A.; Wilson, P.J.M.; Sutherland, H.; Norman, B.P.; Hughes, A.T.; Keenan, C.M.; Milan, A.M.; Sakai, T.; Ranganath, L.R.; Gallagher, J.A.; Bou-Gharios, G.
Conditional targeting in mice reveals that hepatic homogentisate 1,2-dioxygenase activity is essential in reducing circulating homogentisic acid and for effective therapy in the genetic disease alkaptonuria
Hum. Mol. Genet.
28
3928-3939
2019
Homo sapiens (Q93099)
brenda
Sen Gupta, P.S.; Islam, R.N.U.; Banerjee, S.; Nayek, A.; Rana, M.K.; Bandyopadhyay, A.K.
Screening and molecular characterization of lethal mutations of human homogentisate 1,2 dioxigenase
J. Biomol. Struct. Dyn.
39
1661-1671
2021
Homo sapiens (Q93099)
brenda
Wilson, P.J.M.; Ranganath, L.R.; Bou-Gharios, G.; Gallagher, J.A.; Hughes, J.H.
Expression of tyrosine pathway enzymes in mice demonstrates that homogentisate 1,2-dioxygenase deficiency in the liver is responsible for homogentisic acid-derived ochronotic pigmentation
JIMD Rep.
58
52-60
2021
Mus musculus (O09173)
brenda