Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 1.13.11.15 extracted from

  • Boldt, Y.R.; Whiting, A.K.; Wagner, M.L.; Sadowsky, M.J.; Que, L.Jr.; Wackett, L.P.
    Manganese(II) active site mutants of 3,4-dihydroxyphenylacetate 2,3-dioxygenase from Arthrobacter globiformis strain CM-2 (1997), Biochemistry, 36, 2147-2153.
    View publication on PubMed
Search for more literature for 1.13.11.15

Protein Variants

Protein Variants Comment Organism
E266Q specific activity is less than 0.1% of that of the wild-type enzyme, binds 33% of the wild-type level of manganese Arthrobacter globiformis
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 Arthrobacter globiformis
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 Arthrobacter globiformis
H42A 97% of wild-type activity at 18°C, 30% of wild-type activity at 37°C Arthrobacter globiformis

Metals/Ions

Metals/Ions Comment Organism Structure
Manganese enzyme is dependent on manganese, the conserved residues H155, H1214 and E266 ligate manganese Arthrobacter globiformis

Organism

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

Purification (Commentary)

Purification (Comment) Organism
wild-type and mutant enzymes Arthrobacter globiformis

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
0.01
-
-
 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
-
 ?