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Literature summary for 1.13.11.15 extracted from

  • Emerson, J.P.; Wagner, M.L.; Reynolds, M.F.; Que, L.; Sadowsky, M.J.; Wackett, L.P.
    The role of histidine 200 in MndD, the Mn(II)-dependent 3,4-dihydroxyphenylacetate 2,3-dioxygenase from Arthrobacter globiformis CM-2, a site-directed mutagenesis study (2005), J. Biol. Inorg. Chem., 10, 751-760.
    View publication on PubMed
Search for more literature for 1.13.11.15

Protein Variants

Protein Variants Comment Organism
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 Arthrobacter globiformis
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 Arthrobacter globiformis
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 Arthrobacter globiformis
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 Arthrobacter globiformis

Inhibitors

Inhibitors Comment Organism Structure
4-nitrocatechol
-
 Arthrobacter globiformis

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.012
-
 3,4-Dihydroxyphenylacetate 23°C, pH 7.5, mutant enzyme H200A Arthrobacter globiformis
0.017
-
 3,4-Dihydroxyphenylacetate 23°C, pH 7.5, mutant enzyme H200E Arthrobacter globiformis
0.018
-
 3,4-Dihydroxyphenylacetate 23°C, pH 7.5, mutant enzyme H200Q Arthrobacter globiformis
0.021
-
 3,4-Dihydroxyphenylacetate 23°C, pH 7.5, mutant enzyme H200N Arthrobacter globiformis
0.021
-
 3,4-Dihydroxyphenylacetate 23°C, pH 7.5, wild-type enzyme Arthrobacter globiformis

Metals/Ions

Metals/Ions Comment Organism Structure
Mn wild-type enzyme amd mutant enzymes H200A and H200Q: 0.6 Mn per monomer. Mutant enzyme H200E: 0.3 Mn per monomer. Mutent enzyme H200N: 0.4 MN per monomer Arthrobacter globiformis

Organism

Organism UniProt Comment Textmining
Arthrobacter globiformis
-
 CM-2
-
Arthrobacter globiformis CM-2
-
 CM-2
-

Purification (Commentary)

Purification (Comment) Organism
wild-type enzyme and H200 mutants Arthrobacter globiformis

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3,4-dihydroxyphenylacetate + O2
-
 Arthrobacter globiformis 2-hydroxy-5-carboxymethylmuconate semialdehyde
-
 ?
3,4-dihydroxyphenylacetate + O2
-
 Arthrobacter globiformis CM-2 2-hydroxy-5-carboxymethylmuconate semialdehyde
-
 ?

Synonyms

Synonyms Comment Organism
Mn(II)-dependent 3,4-dihydroxyphenylacetate 2,3-dioxygenase
-
 Arthrobacter globiformis

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
0.067
-
 3,4-Dihydroxyphenylacetate 23°C, pH 7.5, mutant enzyme H200A Arthrobacter globiformis
2.67
-
 3,4-Dihydroxyphenylacetate 23°C, pH 7.5, mutant enzyme H200N Arthrobacter globiformis
3.6
-
 3,4-Dihydroxyphenylacetate 23°C, pH 7.5, mutant enzyme H200Q Arthrobacter globiformis
4.6
-
 3,4-Dihydroxyphenylacetate 23°C, pH 7.5, wild-type enzyme Arthrobacter globiformis

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7 8 mutant enzyme H200N and H200Q Arthrobacter globiformis
8 9 wild-type enzyme Arthrobacter globiformis

Ki Value [mM]

Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
additional information
-
 additional information Ki-values for 4-nitrocatechol for the H200A, H200E, H200N and H200Q variants are between 0.015 and 0.025 mM Arthrobacter globiformis