4.1.3.43: 4-hydroxy-2-oxohexanoate aldolase
This is an abbreviated version!
For detailed information about 4-hydroxy-2-oxohexanoate aldolase, go to the full flat file.
Reaction
Synonyms
BphI, TTHB246
ECTree
4.1.3.43 4-hydroxy-2-oxohexanoate aldolaseAdvanced search results
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results (Engineering
Engineering on EC 4.1.3.43 - 4-hydroxy-2-oxohexanoate aldolase
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PROTEIN VARIANTS 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
G322A
-
channels acetaldehyde with similar efficiency to wild-type, 30% lowered efficiency of isobutyraldehyde channeling
G323A
-
channels acetaldehyde with similar efficiency to wild-type, unable to channel isobutyraldehyde
G323L
-
63% channeling efficiency for acetaldehyde, unable to channel propionaldehyde
H20A
H20S
-
mutant generated by site-directed mutagenesis, pH profiles show the dependence of enzyme activity on hydroxide concentration
L87A
-
mutant generated by site-directed mutagenesis, variant exhibits a 40fold preference for propionaldehyde over acetaldehyde in contrast to wild type with similar specificities for acetaldehyde and propionaldehyde
L87N/Y290F
-
exhibits stereoselectivity opposite to that of the wild type and alkyl chain length of the aldehyde does not affect stereochemical control
L87W/Y290F
-
exhibits stereoselectivity opposite to that of the wild type and alkyl chain length of the aldehyde does not affect stereochemical control
L89A
R16A
-
mutant generated by site-directed mutagenesis, no detectable aldol cleavage and pyruvate R-proton exchange, supporting the role of Arg-16 in stabilizing a pyruvate enolate intermediate
Y290F
Y290S
-
mutant generated by site-directed mutagenesis, mutation results in a loss of stereochemical control as the variant is able to utilize substrates with R and S configurations at C4 with similar kinetic parameters
A324G
increase of channeling efficiency of propionaldehyde to a value comparable to that of acetaldehyde
additional information
H20A
-
mutant generated by site-directed mutagenesis, pH profiles show the dependence of enzyme activity on hydroxide concentration
H20A
-
reduction of acetaldehyde and propionaldehyde channeling by more than 70%
L89A
-
mutant generated by site-directed mutagenesis, specificity constant of this variant in the aldol addition reaction using pentaldehyde is increased approx. 50fold, making it more catalytically efficient for pentaldehyde utilization compared to the wild-type utilization of the natural substrate, acetaldehyde
L89A
-
reduction in channeling efficiency of 30% for all aldehydes tested
Y290F
-
mutant generated by site-directed mutagenesis, mutation results in a loss of stereochemical control as the variant is able to utilize substrates with R and S configurations at C4 with similar kinetic parameters
Y290F
-
mutant is able to completely degrade racemic mixtures of 4-hydroxy-2-oxoacids i.e. is not stereospecific
Y290F
-
reduction in channeling efficiency of 30% for all aldehydes tested
additional information
-
all mutations created by site specific mutagenesis
additional information
-
mutants created by site-specific mutagenesis
