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Literature summary extracted from

  • Maenpuen, S.; Amornwatcharapong, W.; Krasatong, P.; Sucharitakul, J.; Palfey, B.A.; Yuthavong, Y.; Chitnumsub, P.; Leartsakulpanich, U.; Chaiyen, P.
    Kinetic mechanism and the rate-limiting step of Plasmodium vivax serine hydroxymethyltransferase (2015), J. Biol. Chem., 290, 8656-8665.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
2.1.2.1 recombinant expression in Escherichia coli strain BL21(DE3) Plasmodium vivax

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
2.1.2.1 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]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
2.1.2.1 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/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2.1.2.1 5,10-methylenetetrahydrofolate + glycine + H2O Plasmodium vivax
-
 tetrahydrofolate + L-serine
-
 r
2.1.2.1 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 ?
-
 ?
2.1.2.1 tetrahydrofolate + L-serine Plasmodium vivax
-
 5,10-methylenetetrahydrofolate + glycine + H2O
-
 r

Organism

EC Number Organism UniProt Comment Textmining
2.1.2.1 Plasmodium vivax
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
2.1.2.1 recombinant enzyme from Escherichia coli strain BL21(DE3) by polyethyleneimine precipitation, anion and cation exchange chromatography Plasmodium vivax

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.1.2.1 5,10-methylenetetrahydrofolate + glycine + H2O
-
 Plasmodium vivax tetrahydrofolate + L-serine
-
 r
2.1.2.1 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 ?
-
 ?
2.1.2.1 tetrahydrofolate + L-serine
-
 Plasmodium vivax 5,10-methylenetetrahydrofolate + glycine + H2O
-
 r

Synonyms

EC Number Synonyms Comment Organism
2.1.2.1 serine hydroxymethyltransferase
-
 Plasmodium vivax
2.1.2.1 SHMT
-
 Plasmodium vivax

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
2.1.2.1 25
-
 assay at Plasmodium vivax

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
2.1.2.1 1.09
-
 L-serine pH 7.0-8.0, 25°C Plasmodium vivax

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
2.1.2.1 7 8 assay at Plasmodium vivax

Cofactor

EC Number Cofactor Comment Organism Structure
2.1.2.1 5,10-methylenetetrahydrofolate
-
 Plasmodium vivax
2.1.2.1 pyridoxal 5'-phosphate dependent on Plasmodium vivax
2.1.2.1 tetrahydrofolate
-
 Plasmodium vivax

General Information

EC Number General Information Comment Organism
2.1.2.1 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