4.1.2.40: tagatose-bisphosphate aldolase
This is an abbreviated version!
For detailed information about tagatose-bisphosphate aldolase, go to the full flat file.
Word Map on EC 4.1.2.40
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4.1.2.40
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streptococcus
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aldolases
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pyogenes
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6-phosphate
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lactis
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lactococcus
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phosphotransferase
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phosphoglycolohydroxamate
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fbpas
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phosphoenolpyruvate-dependent
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diastereoisomers
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galactitol
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speb
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analysis
- 4.1.2.40
- streptococcus
- aldolases
- pyogenes
- 6-phosphate
- lactis
- lactococcus
-
phosphotransferase
- phosphoglycolohydroxamate
-
fbpas
-
phosphoenolpyruvate-dependent
-
diastereoisomers
- galactitol
- speb
- analysis
Reaction
Synonyms
aldolase, tagatose 1,6-diphosphate, D-Tagatose 1,6-diphosphate aldolase, D-tagatose-1,6-bisphosphate aldolase, D-Tagatose-1,6-bisphosphate aldolase (class I), D-Tagatose-1,6-bisphosphate aldolase (class II), GatY, LacD, LacD.1, Tagatose 1,6-bisphosphate aldolase, Tagatose bisphosphate aldolase, tagatose-1,6-biphosphate aldolase 2, tagatose-1,6-bisphosphate aldolase, Tagatose-1,6-diphosphate aldolase, Tagatose-bisphosphate aldolase, TBA, TBP aldolase, TDP aldolase
ECTree
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Engineering
Engineering on EC 4.1.2.40 - tagatose-bisphosphate aldolase
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L165E
the mutant shows enhanced substrate specificity toward fructose-1,6-bisphosphate
L165E/L275S
the mutant shows enhanced substrate specificity toward fructose-1,6-bisphosphate
L275S
the mutant shows enhanced substrate specificity toward fructose-1,6-bisphosphate
K204A
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mutation results in more than 98% decrease in aldolase activity
additional information
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construction of chimeras of isoforms LacD.1 and LacD.2. The C-terminus of LacD.1 contributes to its differential enzymatic activity, as replacing of its C-terminal half with 162 amino acid residues from the C-terminus of LacD.2 leads to an enzyme very similarly to LacD.2 in the cleavage of tagatose bisphosphate but over 3 times more efficient than LacD.2 at cleaving fructose bisphosphate. In addition, loop 1 and turn 2 influence the differential enzymatic activity of LacD.1
additional information
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construction of chimeras of isoforms LacD.1 and LacD.2. The C-terminus of LacD.1 contributes to its differential enzymatic activity, as replacing of its C-terminal half with 162 amino acid residues from the C-terminus of LacD.2 leads to an enzyme very similarly to LacD.2 in the cleavage of tagatose bisphosphate but over 3 times more efficient than LacD.2 at cleaving fructose bisphosphate. In addition, loop 1 and turn 2 influence the differential enzymatic activity of LacD.1
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