1.13.11.5: homogentisate 1,2-dioxygenase
This is an abbreviated version!
For detailed information about homogentisate 1,2-dioxygenase, go to the full flat file.
Word Map on EC 1.13.11.5
-
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
- 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
Reaction
Synonyms
EC 1.13.1.5, EC 1.99.2.5, ElHDO, HgD, HGDO, HGO, HGOa, HGOb, HmgA, homogentisate 1,2 dioxigenase, homogentisate 1,2 dioxygenase, homogentisate 1,2-dioxygenase, homogentisate dioxygenase, homogentisate oxidase, homogentisate oxygenase, homogentisate phytyl-transferase, homogentisic acid 1,2-dioxygenase, homogentisic acid oxidase, homogentisic acid oxygenase, homogentisic oxygenase, homogentisicase, HPT, HTO
ECTree
1.13.11.5 homogentisate 1,2-dioxygenaseAdvanced search results
results (
results (Engineering
Engineering on EC 1.13.11.5 - homogentisate 1,2-dioxygenase
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
top
PROTEIN VARIANTS 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
G272E
ADH05034.1
mutation is responsible for pigment overproduction in Bacillus thuringiensis BMB181
R378G
A122D
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
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
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
V300G
W60G
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
-
additional information
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
-
alkaptonuric mouse lacks enzyme activity and have recessive mutation aku, mapped to chromosome 16, inbred strain C57BLG/J is heterozygous for the aku mutation
