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Literature summary for 1.4.1.20 extracted from

  • Ye, L.; Toh, H.; Yang, Y.; Adams, J.; Snajdrova, R.; Li, Z.
    Engineering of amine dehydrogenase for asymmetric reductive amination of ketone by evolving Rhodococcus phenylalanine dehydrogenase (2015), ACS Catal., 5, 1119-1122 .
No PubMed abstract available
Search for more literature for 1.4.1.20

Protein Variants

Protein Variants Comment Organism
K66Q/S149G/N262C the mutant shows activity with phenylacetone and 4-phenyl-2-butanone Rhodococcus sp.

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.4
-
 4-phenyl-2-butanone mutant enzyme K66Q/S149G/N262C, at pH 9.6 and 30°C Rhodococcus sp.
4
-
 phenylacetone mutant enzyme K66Q/S149G/N262C, at pH 9.6 and 30°C Rhodococcus sp.

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
L-phenylalanine + H2O + NAD+ Rhodococcus sp.
-
 phenylpyruvate + NH3 + NADH + H+
-
 ?

Organism

Organism UniProt Comment Textmining
Rhodococcus sp. Q59771
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
4-phenyl-2-butanone + NH3 + NADH + H+ substrate for mutant enzyme K66Q/S149G/N262C Rhodococcus sp. (R)-1-methyl-3-phenylpropylamine + H2O + NAD+
-
 ?
L-phenylalanine + H2O + NAD+
-
 Rhodococcus sp. phenylpyruvate + NH3 + NADH + H+
-
 ?
phenylacetone + NH3 + NADH + H+ substrate for mutant enzyme K66Q/S149G/N262C Rhodococcus sp. (R)-amphetamine + H2O + NAD+
-
 ?

Synonyms

Synonyms Comment Organism
PheDH
-
 Rhodococcus sp.

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
0.7
-
 phenylacetone mutant enzyme K66Q/S149G/N262C, at pH 9.6 and 30°C Rhodococcus sp.
0.72
-
 4-phenyl-2-butanone mutant enzyme K66Q/S149G/N262C, at pH 9.6 and 30°C Rhodococcus sp.

Cofactor

Cofactor Comment Organism Structure
NAD+
-
 Rhodococcus sp.

kcat/KM [mM/s]

kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
0.18
-
 phenylacetone mutant enzyme K66Q/S149G/N262C, at pH 9.6 and 30°C Rhodococcus sp.
0.5
-
 4-phenyl-2-butanone mutant enzyme K66Q/S149G/N262C, at pH 9.6 and 30°C Rhodococcus sp.