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Literature summary for 1.13.11.72 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
Search for more literature for 1.13.11.72

Protein Variants

Protein Variants Comment Organism
K16A loss of enzymic activity Streptomyces viridochromogenes
R90A large decrease in ratio kcat/Km, mutant cannot be saturated in O2 Streptomyces viridochromogenes
R90K slight decrease in ratio kcat/Km Streptomyces viridochromogenes
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]

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

Organism

Organism UniProt Comment Textmining
Streptomyces viridochromogenes Q5IW40
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2-hydroxyethylphosphonate + O2
-
 Streptomyces viridochromogenes hydroxymethylphosphonate + formate
-
 ?
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]

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

kcat/KM [mM/s]

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