Cloned (Comment) | Organism |
---|---|
recombinant expression in Escherichia coli strain BL21(DE3) | Plasmodium vivax |
Crystallization (Comment) | Organism |
---|---|
substrate binding structure analysis using crystal structure of the homodimeric PvSHMT in complex with D-serine and formyltetrahydrofolate, PDB ID 4OYT | Plasmodium vivax |
KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
additional information | - |
additional information | kinetic analysis of ternary complex mechanism, determination of ligand binding, transient, single-turnover and bi-substrate steady-state kinetics, detailed overview. The enzyme can bind first to either L-serine or tetrahydrofolate. The dissociation constants for the enzyme-L-serine and enzyme-tetrahydrofolate complexes are 0.18 mM and 0.35 mM, respectively. The kinetic mechanism of PvSHMT occurs via a random-order model and glycine formation is the rate-limiting step of the enzyme reaction | Plasmodium vivax |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
5,10-methylenetetrahydrofolate + glycine + H2O | Plasmodium vivax | - |
tetrahydrofolate + L-serine | - |
r | |
additional information | Plasmodium vivax | serine hydroxymethyltransferase is a pyridoxal 5'-phosphate-dependent enzyme that catalyzes a hydroxymethyl group transfer from L-serine to tetrahydrofolate to yield glycine and 5,10-methylenetetrahydrofolate | ? | - |
? | |
tetrahydrofolate + L-serine | Plasmodium vivax | - |
5,10-methylenetetrahydrofolate + glycine + H2O | - |
r |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Plasmodium vivax | - |
- |
- |
Purification (Comment) | Organism |
---|---|
recombinant enzyme from Escherichia coli strain BL21(DE3) by polyethyleneimine precipitation, anion and cation exchange chromatography | Plasmodium vivax |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
5,10-methylenetetrahydrofolate + glycine + H2O | - |
Plasmodium vivax | tetrahydrofolate + L-serine | - |
r | |
additional information | serine hydroxymethyltransferase is a pyridoxal 5'-phosphate-dependent enzyme that catalyzes a hydroxymethyl group transfer from L-serine to tetrahydrofolate to yield glycine and 5,10-methylenetetrahydrofolate | Plasmodium vivax | ? | - |
? | |
tetrahydrofolate + L-serine | - |
Plasmodium vivax | 5,10-methylenetetrahydrofolate + glycine + H2O | - |
r |
Synonyms | Comment | Organism |
---|---|---|
serine hydroxymethyltransferase | - |
Plasmodium vivax |
SHMT | - |
Plasmodium vivax |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
25 | - |
assay at | Plasmodium vivax |
Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
1.09 | - |
L-serine | pH 7.0-8.0, 25°C | Plasmodium vivax |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
7 | 8 | assay at | Plasmodium vivax |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
5,10-methylenetetrahydrofolate | - |
Plasmodium vivax | |
pyridoxal 5'-phosphate | dependent on | Plasmodium vivax | |
tetrahydrofolate | - |
Plasmodium vivax |
General Information | Comment | Organism |
---|---|---|
physiological function | the enzyme is crucial for deoxythymidylate biosynthesis and a target for antimalarial drug development, the Plasmodium vivax enzyme catalyzes the reaction via a ternary complex mechanism | Plasmodium vivax |