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4.1.2.49: L-allo-threonine aldolase

This is an abbreviated version!
For detailed information about L-allo-threonine aldolase, go to the full flat file.

Word Map on EC 4.1.2.49

Reaction

L-allo-threonine
=
glycine
 +
acetaldehyde

Synonyms

L-allo-TA, L-allo-threonine acetaldehyde-lyase, LATA, ltaA

ECTree

     4 Lyases
         4.1 Carbon-carbon lyases
             4.1.2 Aldehyde-lyases
                4.1.2.49 L-allo-threonine aldolase

Engineering

Engineering on EC 4.1.2.49 - L-allo-threonine aldolase

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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
D168N
mutation reduces the specific activity, which is partially restored by the addition of excess pyridoxal 5'-phosphate to the reaction mixture. The mutant enzyme is able to catalyse the aldol synthesis of L-beta-phenylserine from benzaldehyde and glycine with yields similar to the wild-type enzyme
D168S
mutation reduces the specific activity, which is partially restored by the addition of excess pyridoxal 5'-phosphate to the reaction mixture. The mutant enzyme is able to catalyse the aldol synthesis of L-beta-phenylserine from benzaldehyde and glycine with yields similar to the wild-type enzyme
D168T
mutation reduces the specific activity, which is partially restored by the addition of excess pyridoxal 5'-phosphate to the reaction mixture. The mutant enzyme is able to catalyse the aldol synthesis of L-beta-phenylserine from benzaldehyde and glycine with yields similar to the wild-type enzyme
D168V
mutation reduces the specific activity, which is partially restored by the addition of excess pyridoxal 5'-phosphate to the reaction mixture. The mutant enzyme is able to catalyse the aldol synthesis of L-beta-phenylserine from benzaldehyde and glycine with yields similar to the wild-type enzyme
H128Y
8.4fold increase in activity towards L-threonine and a 2.0fold increase towards L-allo-threonine compared with the wild-type enzyme
H128Y/S292R
3fold and 322fold increased kcat/Km values towards towards L-allo-threonine and L-threonine compared with the wild-type enzyme
K199A
catalytically inactive mutant enzyme
K199R
mutation reduces the specific activity of the enzyme by 5000fold, which can be partially restored by adding an excess of pyridoxal 5'-phosphate to the reaction medium
K224A
mutant enzyme shows properties similar to the wild type enzyme
K51A
mutant enzyme shows properties similar to the wild type enzyme
R171F
loss of specific activity by more than 2000fold. pyridoxal 5'-phosphate-glycine complex is not obtained for the mutant. The mutant is not active in the aldol condensation reaction to produce L-beta-phenylserine
R231A
the mutant enzyme racemizes L-alanine to D-alanine, whereas the wild-type enzyme is not active towards L-alanine
R313H
catalytic activity of the mutant in the retro-aldol cleavage of L-allo-threonine is decreased by 200fold mainly due to increase in Km. Mutation hinders the formation of the quinonoid complex to stabilize the carbanion after initial bond cleavage. L-beta-Phenylserine product in the aldol condensation is obtained with the conversion rate similar to the wild-type enzyme
S292R
improved activity towards L-allo-threonine and L-threonine
H128Y
-
8.4fold increase in activity towards L-threonine and a 2.0fold increase towards L-allo-threonine compared with the wild-type enzyme
-
H128Y/S292R
-
3fold and 322fold increased kcat/Km values towards towards L-allo-threonine and L-threonine compared with the wild-type enzyme
-
K199A
-
catalytically inactive mutant enzyme
-
K224A
-
mutant enzyme shows properties similar to the wild type enzyme
-
K51A
-
mutant enzyme shows properties similar to the wild type enzyme
-
S292R
-
improved activity towards L-allo-threonine and L-threonine
-