1.13.11.15: 3,4-dihydroxyphenylacetate 2,3-dioxygenase
This is an abbreviated version!
For detailed information about 3,4-dihydroxyphenylacetate 2,3-dioxygenase, go to the full flat file.
Word Map on EC 1.13.11.15
-
1.13.11.15
-
extradiol
-
catecholate
-
4-nitrocatechol
-
fuscum
-
brevibacterium
-
globiformis
-
manganese-dependent
-
ring-cleaving
-
extradiol-cleaving
-
second-sphere
-
monoanionic
-
hydroperoxo
-
4-hydroxyphenylacetate
-
superoxo
-
alkylperoxo
-
feiii-superoxo
-
manganeseii
-
ortho-dihydroxylated
-
side-on
-
crystallo
- 1.13.11.15
-
extradiol
-
catecholate
- 4-nitrocatechol
- fuscum
-
brevibacterium
- globiformis
-
manganese-dependent
-
ring-cleaving
-
extradiol-cleaving
-
second-sphere
-
monoanionic
-
hydroperoxo
- 4-hydroxyphenylacetate
-
superoxo
-
alkylperoxo
-
feiii-superoxo
-
manganeseii
-
ortho-dihydroxylated
-
side-on
-
crystallo
Reaction
Synonyms
2,3-HPCD, 3,4-dihydroxyphenylacetic acid 2,3-dioxygenase, Bf 2,3-HPCD, DHPAO, Fe-HPCD, Fe-MndD, FeHPCD, homoprotocatechuate 2,3 dioxygenase, homoprotocatechuate 2,3-dioxygenase, homoprotocatechuate dioxygenase, HPADO, HPC 2,3-dioxygenase, HPC dioxygenase, HPCA 2,3-dioxygenase, HPCD, Mn(II)-dependent 3,4-dihydroxyphenylacetate 2,3-dioxygenase, Mn-HPCD, Mn-MndD, MndD, MnHPCD, oxygenase, homoprotocatechuate 2,3-di-, PaDHPAO
ECTree
1.13.11.15 3,4-dihydroxyphenylacetate 2,3-dioxygenaseAdvanced search results
results (
results (Engineering
Engineering on EC 1.13.11.15 - 3,4-dihydroxyphenylacetate 2,3-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
E266Q
-
specific activity is less than 0.1% of that of the wild-type enzyme, binds 33% of the wild-type level of manganese
H155A
-
specific activity is less than 0.1% of that of the wild-type enzyme, binds 0.4% of the wild-type level of manganese
H200A
-
KM-value for 3,4-dihydroxyphenylacetate is 1.75fold lower than wild-type value, kcat for 3,4-dihydroxyphenylacetate is 69fold lower than wild-type value
H200E
-
KM-value for 3,4-dihydroxyphenylacetate is 1.2fold lower than wild-type value, kcat for 3,4-dihydroxyphenylacetate is more than 276fold lower than wild-type value, Mn content per monomer is 2fold lower than in wild-type enzyme
H200N
-
KM-value for 3,4-dihydroxyphenylacetate is identical to wild-type value, kcat for 3,4-dihydroxyphenylacetate is 1.73fold lower than wild-type value, Mn content per monomer is 65% of wild-type value
H200Q
-
KM-value for 3,4-dihydroxyphenylacetate is 1.2fold lower than wild-type value, kcat for 3,4-dihydroxyphenylacetate is 1.3fold lower than wild-type value
H214A
-
specific activity is less than 0.1% of that of the wild-type enzyme, binds 1.8% of the wild-type level of manganese
H42A
-
97% of wild-type activity at 18°C, 30% of wild-type activity at 37°C
E266Q
-
specific activity is less than 0.1% of that of the wild-type enzyme, binds 33% of the wild-type level of manganese
-
H155A
-
specific activity is less than 0.1% of that of the wild-type enzyme, binds 0.4% of the wild-type level of manganese
-
H200A
-
KM-value for 3,4-dihydroxyphenylacetate is 1.75fold lower than wild-type value, kcat for 3,4-dihydroxyphenylacetate is 69fold lower than wild-type value
-
H200E
-
KM-value for 3,4-dihydroxyphenylacetate is 1.2fold lower than wild-type value, kcat for 3,4-dihydroxyphenylacetate is more than 276fold lower than wild-type value, Mn content per monomer is 2fold lower than in wild-type enzyme
-
H200N
-
KM-value for 3,4-dihydroxyphenylacetate is identical to wild-type value, kcat for 3,4-dihydroxyphenylacetate is 1.73fold lower than wild-type value, Mn content per monomer is 65% of wild-type value
-
H200Q
-
KM-value for 3,4-dihydroxyphenylacetate is 1.2fold lower than wild-type value, kcat for 3,4-dihydroxyphenylacetate is 1.3fold lower than wild-type value
-
H214A
-
specific activity is less than 0.1% of that of the wild-type enzyme, binds 1.8% of the wild-type level of manganese
-
H42A
-
97% of wild-type activity at 18°C, 30% of wild-type activity at 37°C
-
H200A
-
Km-value for 3,4-dihydroxyphenylacetate is 6fold lower than wild-type value, kcat for 3,4-dihydroxyphenylacetate is 33.3fold lower than wild-type value
H200E
-
Km-value for 3,4-dihydroxyphenylacetate is 75fold lower than wild-type value, kcat for 3,4-dihydroxyphenylacetate is 11.1fold lower than wild-type value
H200F
H200N
H200Q
-
Km-value for 3,4-dihydroxyphenylacetate is similar to wild-type value, kcat for 3,4-dihydroxyphenylacetate is 2.5fold lower than wild-type value
Y257F
additional information
H200F
-
switch of reaction from extradiol to intradiol cleavage for substrate 2,3-dihydroxybenzoate
H200F
-
Km-value for 3,4-dihydroxyphenylacetate is similar to wild-type value, kcat for 3,4-dihydroxyphenylacetate is 47.6fold lower than wild-type value
H200N
-
Km-value for 3,4-dihydroxyphenylacetate is 3fold lower than wild-type value, kcat for 3,4-dihydroxyphenylacetate is 3.33fold lower than wild-type value
H200N
-
site-directed mutagenesis, catalytic reaction intermediate formation in the mutant differs from the wild-type enzyme, Mössbauer spectral analysis, overview
H200N
variant employs a C4 (para-carbon) pathway to produce a C4-C5 cleavage product
Y257F
site-directed mutagenesis, changes in kinetics for Y257F variant can be attributed to the loss of interactions between substrate and Tyr257, substrate binding structures compared to the wild-type enzyme, overview
Y257F
-
site-directed mutagenesis, the two reaction intermediates formed with the mutant enzyme differ from that of the the wild-type enzyme, substrate binds tightly to Y257F, the intense Mössbauer spectrum of suggests the intermediate is most likely an HPCA quinone-FeII-(hydro)peroxo species. Steady-state and transient kinetic analyses show that steps of the catalytic cycle are slowed by as much as 100fold by the mutation due to failure of Y257F to facilitate the observed distortion of the bound HPCA that is proposed to promote transfer of one electron to O2, Mössbauer spectral analysis, overview
additional information
-
triple mutant in which the three gaps in the sequence are removed does not show a significant change in metal content
additional information
small model including only the most relevant parts of the residues, H155, H214, E267, Y257, directyl coordinated to Fe(II); model insufficient for a proper modeling of the enzymatic reaction
additional information
-
small model including only the most relevant parts of the residues, H155, H214, E267, Y257, directyl coordinated to Fe(II); model insufficient for a proper modeling of the enzymatic reaction
