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

BRENDA support

Literature summary for 1.1.1.1 extracted from

  • Enugala, T.; Morato, M.; Kamerlin, S.; Widersten, M.
    The role of substrate-coenzyme crosstalk in determining turnover rates in Rhodococcus ruber alcohol dehydrogenase (2020), ACS Catal., 10, 9115-9128 .
No PubMed abstract available
Search for more literature for 1.1.1.1

Protein Variants

Protein Variants Comment Organism
F43H site-directed mutagenesis, mutant C1 variant Rhodococcus ruber
F43H/Y54L site-directed mutagenesis, mutant C1B1 variant Rhodococcus ruber
F43T/Y54G/L119Y/F282W site-directed mutagenesis, mutant B1F4 variant Rhodococcus ruber
H39Y/F43H/Y54F/Y294F/W295A site-directed mutagenesis, mutant A2C2B1 variant Rhodococcus ruber
H39Y/F43S/Y294F/W295A site-directed mutagenesis, mutant A2C3 variant Rhodococcus ruber
additional information generation of A2C2B1 variant, A2C3 variant, B1 variant, B1F4 variant, C1 variant, and C1B1 variant, crystal structure comparisons with the wild-type enzyme, overview Rhodococcus ruber
W295A site-directed mutagenesis, mutant A1 variant Rhodococcus ruber
Y294F/W295A site-directed mutagenesis, compared to the wild-type enzyme, a shift in enantioselectivity and differences in catalytic activity with 4-phenyl-2-butanol are observed Rhodococcus ruber
Y294F/W295A site-directed mutagenesis, mutant A2 variant Rhodococcus ruber
Y54G/L119Y site-directed mutagenesis, mutant B1 variant Rhodococcus ruber

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
 additional information pre-steady-state and Michaelis-Menten steady-state kinetics, molecular dynamics simulations of enzyme-substrate interactions in the Michaelis complexes of wild-type ADH-A and Y294F/W295A double mutant. Interdependency between substrate/product and the cofactor in the ternary complex is determined, which directly affects the NADH dissociation rates, therefore, this substrate-coenzyme crosstalk plays a direct role in determining the turnover rates. Model of the kinetic mechanism of ADH-A, overview Rhodococcus ruber

Metals/Ions

Metals/Ions Comment Organism Structure
Zn2+ two essential zinc ions Rhodococcus ruber

Organism

Organism UniProt Comment Textmining
Rhodococcus ruber
-
-
-
Rhodococcus ruber DSM 44541
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
(R)-1-phenyl-1-butanol + NAD+ no substrate of mutant B1 Rhodococcus ruber 1-phenylbutan-1-one + NADH + H+
-
 r
(R)-1-phenyl-1-butanol + NAD+ no substrate of mutant B1 Rhodococcus ruber DSM 44541 1-phenylbutan-1-one + NADH + H+
-
 r
(R)-1-phenyl-1-propanol + NAD+
-
 Rhodococcus ruber 1-phenyl-1-propanone + NADH + H+
-
 r
(R)-1-phenyl-2-butanol + NAD+
-
 Rhodococcus ruber 1-phenylbutan-2-one + NADH + H+
-
 r
(R)-1-phenylethanol + NAD+
-
 Rhodococcus ruber acetophenone + NADH + H+
-
 r
(R)-1-phenylethanol + NAD+
-
 Rhodococcus ruber DSM 44541 acetophenone + NADH + H+
-
 r
(R)-4-phenyl-2-butanol + NAD+
-
 Rhodococcus ruber 4-phenylbutan-2-one + NADH + H+
-
 r
(S)-1-phenyl-1-butanol + NAD+ no substrate of mutant B1 Rhodococcus ruber 1-phenylbutan-1-one + NADH + H+
-
 r
(S)-1-phenyl-1-propanol + NAD+
-
 Rhodococcus ruber 1-phenyl-1-propanone + NADH + H+
-
 r
(S)-1-phenyl-2-butanol + NAD+
-
 Rhodococcus ruber 1-phenylbutan-2-one + NADH + H+
-
 r
(S)-1-phenylethanol + NAD+
-
 Rhodococcus ruber acetophenone + NADH + H+
-
 r
(S)-1-phenylethanol + NAD+
-
 Rhodococcus ruber DSM 44541 acetophenone + NADH + H+
-
 r
(S)-4-phenyl-2-butanol + NAD+
-
 Rhodococcus ruber 4-phenylbutan-2-one + NADH + H+
-
 r
2-butanol + NAD+
-
 Rhodococcus ruber 2-butanone + NADH + H+
-
 r
2-butanol + NAD+
-
 Rhodococcus ruber DSM 44541 2-butanone + NADH + H+
-
 r
additional information substrate specificities and enantioselectivities of wild-type and mutant enzymes, overview. Molecular dynamics of wild-type ADH-A (PDB ID 3jv7) and the A2 variant (PDB ID 5o8q) in complex with alcohols (R)- and (S)-4-phenyl-2-butanol Rhodococcus ruber ?
-
-
additional information substrate specificities and enantioselectivities of wild-type and mutant enzymes, overview. Molecular dynamics of wild-type ADH-A (PDB ID 3jv7) and the A2 variant (PDB ID 5o8q) in complex with alcohols (R)- and (S)-4-phenyl-2-butanol Rhodococcus ruber DSM 44541 ?
-
-

Subunits

Subunits Comment Organism
dimer
-
 Rhodococcus ruber

Synonyms

Synonyms Comment Organism
ADH
-
 Rhodococcus ruber
ADH-A
-
 Rhodococcus ruber
SADH
-
 Rhodococcus ruber

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
30
-
 assay at Rhodococcus ruber

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
8
-
 assay at Rhodococcus ruber

Cofactor

Cofactor Comment Organism Structure
NAD+
-
 Rhodococcus ruber
NADH cofactor binding analysis with wild-type and mutant enzymes, crystal structure analysis, overview Rhodococcus ruber

General Information

General Information Comment Organism
additional information molecular dynamics simulations of enzyme-substrate interactions in the Michaelis complexes of wild-type ADH-A and Y294F/W295A double mutant. Interdependency between substrate/product and the cofactor in the ternary complex is determined, which directly affects the NADH dissociation rates, therefore, this substrate-coenzyme crosstalk plays a direct role in determining the turnover rates. Molecular dynamics of wild-type ADH-A (PDB ID 3jv7) and the A2 variant (PDB ID 5o8q) in complex with alcohols (R)- and (S)-4-phenyl-2-butanol Rhodococcus ruber