2.6.1.52: phosphoserine transaminase
This is an abbreviated version!
For detailed information about phosphoserine transaminase, go to the full flat file.
Reaction
Synonyms
3-O-phospho-L-serine:2-oxoglutarate aminotransferase, 3-phosphoserine aminotransferase, AspAT, AtPSAT, AtPSAT1, BCIR PSAT, bmPSAT, EhPSAT, hydroxypyruvic phosphate-glutamic transaminase, L-phosphoserine aminotransferase, phosphohydroxypyruvate transaminase, phosphohydroxypyruvic-glutamic transaminase, phosphoserine aminotransferase, phosphoserine aminotransferase 1, phosphoserine aminotransferase1, phosphoserine aminotransferase2, phosphoserine aminotransferases, PSAT, PSAT alpha, PSAT beta, PSAT-BALC, PSAT-BCIRA, PSAT-ECOLI, PSAT1, PSAT2, PSerAT, serC, sll1559
ECTree
2.6.1.52 phosphoserine transaminaseAdvanced search results
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results (Engineering
Engineering on EC 2.6.1.52 - phosphoserine transaminase
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PROTEIN VARIANTS 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
W101A
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about 5% of wild-type activity, with very little global conformational change upon the mutation. An average minimum root mean square fluctuation per residue is observed for the wild-type protein as compared to mutants. In mutant W101A, there are no big fluctuations but the stacking interaction is lost due to side chain truncation
W101F
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about 70% of wild-type activity, with very little global conformational change upon the mutation. An average minimum root mean square fluctuation per residue is observed for the wild-type protein as compared to mutants. The stacking interaction for mutants W101F and W101H are not as prominent as for the wild-type protein
W101H
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about 20% of wild-type activity, with very little global conformational change upon the mutation. An average minimum root mean square fluctuation per residue is observed for the wild-type protein as compared to mutants. The stacking interaction for mutants W101F and W101H are not as prominent as for the wild-type protein
R42W
site-directed mutagenesis, the mutant exhibits high activity toward L-homoserine with a low activity toward L-phosphoserine
R42W/R77W
R42W/R77WH328E
site-directed mutagenesis, very low activity with L-homoserine
R42W/R77WH328K
site-directed mutagenesis, no activity with L-homoserine
additional information
R42W/R77W
site-directed mutagenesis, best engineered mutant showing 4.2fold increased activity with L-homoserine compared to wild-type enzyme, the activity toward the natural substrate L-phosphoserine is highly reduced in the mutant enzyme
additional information
PSAT1-silenced lines (ts-psat1.1 and ts-psat1.2) are generated for functional characterization using a microRNA-based approach. Overexpression of the artificial PSAT1-silencing construct in Arabidopsis thaliana leads to a significant reduction of PSAT1 expression, which subsequently results in a strong inhibition of growth. The expression of the PSAT2 gene is unaltered in PSAT1-silenced plants, phenotype, overview
additional information
PSAT1-silenced lines (ts-psat1.1 and ts-psat1.2) are generated for functional characterization using a microRNA-based approach. Overexpression of the artificial PSAT1-silencing construct in Arabidopsis thaliana leads to a significant reduction of PSAT1 expression, which subsequently results in a strong inhibition of growth. The expression of the PSAT2 gene is unaltered in PSAT1-silenced plants, phenotype, overview
additional information
PSAT1-silenced lines (ts-psat1.1 and ts-psat1.2) are generated for functional characterization using a microRNA-based approach. The expression of the PSAT2 gene is unaltered in PSAT1-silenced plants, phenotype, overview
additional information
PSAT1-silenced lines (ts-psat1.1 and ts-psat1.2) are generated for functional characterization using a microRNA-based approach. The expression of the PSAT2 gene is unaltered in PSAT1-silenced plants, phenotype, overview
additional information
deletion of the 45 N-terminal residues in mutant EhPSAT_DELTA45 results in an inactive protein, the structure shows a dimeric arrangement drastically different from that of the wild-type protein, with the two monomers translated and rotated by almost 180° with respect to each other, causing a rearrangement of the active site to which cofactor PLP is unable to bind. Deletions of first N-terminal 15 (EhPSAT_DELTA15) and four 11th to 14th residues (EhPSAT_DELTA4) yield up to 98% and 90% decrease in activity, respectively. Absence of aldimine linkage between PLP-Lys in the crystal structure of EhPSAT_DELTA4 mutant explains the decrease in activity and describes the importance of these N-terminal residues
additional information
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deletion of the 45 N-terminal residues in mutant EhPSAT_DELTA45 results in an inactive protein, the structure shows a dimeric arrangement drastically different from that of the wild-type protein, with the two monomers translated and rotated by almost 180° with respect to each other, causing a rearrangement of the active site to which cofactor PLP is unable to bind. Deletions of first N-terminal 15 (EhPSAT_DELTA15) and four 11th to 14th residues (EhPSAT_DELTA4) yield up to 98% and 90% decrease in activity, respectively. Absence of aldimine linkage between PLP-Lys in the crystal structure of EhPSAT_DELTA4 mutant explains the decrease in activity and describes the importance of these N-terminal residues
additional information
-
deletion of the 45 N-terminal residues in mutant EhPSAT_DELTA45 results in an inactive protein, the structure shows a dimeric arrangement drastically different from that of the wild-type protein, with the two monomers translated and rotated by almost 180° with respect to each other, causing a rearrangement of the active site to which cofactor PLP is unable to bind. Deletions of first N-terminal 15 (EhPSAT_DELTA15) and four 11th to 14th residues (EhPSAT_DELTA4) yield up to 98% and 90% decrease in activity, respectively. Absence of aldimine linkage between PLP-Lys in the crystal structure of EhPSAT_DELTA4 mutant explains the decrease in activity and describes the importance of these N-terminal residues
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additional information
phosphoserine aminotransferase (SerC) from Escherichia coli strain MG1655 is engineered to catalyze the deamination of homoserine to 4-hydroxy-2-oxobutyrate, a key reaction in producing 1,3-propanediol (1,3-PDO) from glucose in a distinct glycerol-independent metabolic pathway. An computation-based rational approach is used to change the substrate specificity of SerC from L-phosphoserine to L-homoserine, molecular dynamics simulations and virtual screening are combined to predict mutation sites. The coexpression of best mutant SerCR42W/R77W with Escherichia coli pyruvate decarboxylase and alcohol dehydrogenase results in production of 3.03 g/l of 1,3-PDO in fed-batch fermentation, which is 13fold higher than in the wild-type strain. Method evaluation, overview
additional information
-
phosphoserine aminotransferase (SerC) from Escherichia coli strain MG1655 is engineered to catalyze the deamination of homoserine to 4-hydroxy-2-oxobutyrate, a key reaction in producing 1,3-propanediol (1,3-PDO) from glucose in a distinct glycerol-independent metabolic pathway. An computation-based rational approach is used to change the substrate specificity of SerC from L-phosphoserine to L-homoserine, molecular dynamics simulations and virtual screening are combined to predict mutation sites. The coexpression of best mutant SerCR42W/R77W with Escherichia coli pyruvate decarboxylase and alcohol dehydrogenase results in production of 3.03 g/l of 1,3-PDO in fed-batch fermentation, which is 13fold higher than in the wild-type strain. Method evaluation, overview
additional information
-
phosphoserine aminotransferase (SerC) from Escherichia coli strain MG1655 is engineered to catalyze the deamination of homoserine to 4-hydroxy-2-oxobutyrate, a key reaction in producing 1,3-propanediol (1,3-PDO) from glucose in a distinct glycerol-independent metabolic pathway. An computation-based rational approach is used to change the substrate specificity of SerC from L-phosphoserine to L-homoserine, molecular dynamics simulations and virtual screening are combined to predict mutation sites. The coexpression of best mutant SerCR42W/R77W with Escherichia coli pyruvate decarboxylase and alcohol dehydrogenase results in production of 3.03 g/l of 1,3-PDO in fed-batch fermentation, which is 13fold higher than in the wild-type strain. Method evaluation, overview
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