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Literature summary extracted from

  • Peck, S.C.; Cooke, H.A.; Cicchillo, R.M.; Malova, P.; Hammerschmidt, F.; Nair, S.K.; van der Donk, W.A.
    Mechanism and substrate recognition of 2-hydroxyethylphosphonate dioxygenase (2011), Biochemistry, 50, 6598-6605.
    View publication on PubMedView publication on EuropePMC

Protein Variants

EC Number Protein Variants Comment Organism
1.13.11.72 K16A loss of enzymic activity Streptomyces viridochromogenes
1.13.11.72 R90A large decrease in ratio kcat/Km, mutant cannot be saturated in O2 Streptomyces viridochromogenes
1.13.11.72 R90K slight decrease in ratio kcat/Km Streptomyces viridochromogenes
1.13.11.72 Y98F large decrease in ratio kcat/Km, mutant cannot be saturated in O2. Mutant produces methylphosphonate as a minor side product Streptomyces viridochromogenes

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.13.11.72 0.0098
-
 2-hydroxyethylphosphonate wild-type, pH 7.5, 20°C Streptomyces viridochromogenes
1.13.11.72 0.033
-
 O2 wild-type, pH 7.5, 20°C Streptomyces viridochromogenes
1.13.11.72 0.06
-
 2-hydroxyethylphosphonate mutant R90K, pH 7.5, 20°C Streptomyces viridochromogenes
1.13.11.72 0.1
-
 O2 mutant R90K, pH 7.5, 20°C Streptomyces viridochromogenes
1.13.11.72 0.69
-
 2-hydroxyethylphosphonate mutant R90A, pH 7.5, 20°C Streptomyces viridochromogenes
1.13.11.72 0.8
-
 2-hydroxyethylphosphonate mutant Y98F, pH 7.5, 20°C Streptomyces viridochromogenes

Organism

EC Number Organism UniProt Comment Textmining
1.13.11.72 Streptomyces viridochromogenes Q5IW40
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.13.11.72 2-hydroxyethylphosphonate + O2
-
 Streptomyces viridochromogenes hydroxymethylphosphonate + formate
-
 ?
1.13.11.72 additional information proper binding of 2-hydroxyethylphosphonate is important for O2 activation and the enzyme uses a compulsory binding order with 2-hydroxyethylphosphonate binding before O2. In the mechanism, a hydroperoxylation process is followed by a Criegee rearrangement and hydrolysis to form hydroxymethylphosphonate. Thereafter, the P-C bond in the product can be transiently broken, generating phosphite and formaldehyde in the active site of the enzyme. If the formaldehyde is able to rotate along the C=O bond, then phosphite can attack either face of the carbonyl group resulting in a loss of stereochemistry Streptomyces viridochromogenes ?
-
 ?

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
1.13.11.72 0.35
-
 2-hydroxyethylphosphonate wild-type, pH 7.5, 20°C Streptomyces viridochromogenes
1.13.11.72 0.81
-
 2-hydroxyethylphosphonate mutant R90K, pH 7.5, 20°C Streptomyces viridochromogenes

kcat/KM [mM/s]

EC Number kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
1.13.11.72 0.1
-
 O2 mutant R90A, pH 7.5, 20°C Streptomyces viridochromogenes
1.13.11.72 0.74
-
 O2 mutant Y98F, pH 7.5, 20°C Streptomyces viridochromogenes
1.13.11.72 8.1
-
 O2 mutant R90K, pH 7.5, 20°C Streptomyces viridochromogenes
1.13.11.72 11
-
 O2 wild-type, pH 7.5, 20°C Streptomyces viridochromogenes
1.13.11.72 13
-
 2-hydroxyethylphosphonate mutant R90K, pH 7.5, 20°C Streptomyces viridochromogenes
1.13.11.72 36
-
 2-hydroxyethylphosphonate wild-type, pH 7.5, 20°C Streptomyces viridochromogenes