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2.1.2.1: glycine hydroxymethyltransferase

This is an abbreviated version!
For detailed information about glycine hydroxymethyltransferase, go to the full flat file.

Word Map on EC 2.1.2.1

Reaction

5,10-methylenetetrahydrofolate
+
glycine
 +
H2O
=
tetrahydrofolate
 +
L-serine

Synonyms

AtSHMT3, bsSHMT, bstSHMT, EC 4.1.2.6, eSHMT, GlyA, GlyA protein, glycine hydroxymethyltransferrase, hSHMT, L-serine hydroxymethyltransferase, mitochondrial serine hydroxymethyltransferase, MJ1597, PvSHMT, Rhg4, serine hydroxymethyl transferase, serine hydroxymethylase hydroxymethyltransferase, serine, serine hydroxymethyltransferase, serine hydroxymethyltransferase 1, serine hydroxymethyltransferase 2, serine hydroxymethyltransferase 2alpha, serine transhydroxymethylase, serine:H4F hydroxymethyltransferase, serine:tetrahydrofolate hydroxymethyltransferase, SHM1, SHM2, SHMT, SHMT-1, SHMT-L, SHMT-S, SHMT08, SHMT1, SHMT2, SHMT2alpha, SHMT3, zcSHMT, zebrafish cytosolic serine hydroxymethyltransferase, zebrafish mitochondiral serine hydroxymethyltransferase, zmSHMT

ECTree

     2 Transferases
         2.1 Transferring one-carbon groups
             2.1.2 Hydroxymethyl-, formyl- and related transferases
                2.1.2.1 glycine hydroxymethyltransferase

General Stability

General Stability on EC 2.1.2.1 - glycine hydroxymethyltransferase

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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
2-mercaptoethanol stabilizes
above 6 M urea the dichrpoic activity is reduced significantly with a transition midpoint at 2.56 M. This process is completely reversible
-
bsSHMT has six unconserved lysine residues in C-terminal domain which render it more resistant to alkaline denaturation. Chemical modification of lysine side chains results in stabilization of monomers
-
dialysis inactivates
-
DTT stabilizes
EDTA stabilizes
folate stabilizes
-
glycine betaine protects the ApSHMT enzyme activity in vitro
guanidinium chloride-induced two-step unfolding of SHM1 with the first step being dissociation of dimer into apomonomer at low denaturant concentrations followed by unfolding of the stabilized monomer at higher denaturant concentrations, SHM1
guanidinium chloride-induced two-step unfolding of SHM1 with the first step being dissociation of dimer into apomonomer at low denaturant concentrations followed by unfolding of the stabilized monomer at higher denaturant concentrations, SHM2
KCl, NaCl or LiCl: denaturation, folate protects
-
L-serine stabilizes
pyridoxal 5'-phosphate stabilizes
tetrahydrofolate stabilizes
-
the kcat value of the enzyme in phosphate buffer is about 60% of that measured in HEPES buffer
-
unlike the wild-type enzyme bsSHMT, which undergoes dissociation of native dimer into monomers at low guanidinium chloride concentrations, resulting in a non-cooperative unfolding of the enzyme, its chimera bsbstc, having the C-terminal domain of bstSHMT is resistant to low guanidinium chloride concentration and shows a guanidinium-chloride-induced cooperative unfolding from native dimer to unfolded monomer. The wild-type dimeric bstSHMT is resistant to low guanidinium chloride concentrations and shows a guanidinium chloride-induced cooperative unfolding, whereas its chimera bstbsc, having the C-terminal domain of bsSHMT, shows dissociation of native dimer into monomer at low guanidinium chloride concentrations and a guanidinium-induced non-cooperative unfolding. The C-terminal domain of dimeric SHMT plays a vital role in stabilization of the oligomeric structure of the native enzyme hence modulating its unfolding pathway
urea-induced two-step unfolding of SHM1 with the first step being dissociation of dimer into apomonomer at low denaturant concentrations followed by unfolding of the stabilized monomer at higher denaturant concentrations. The enzyme-bound pyridoxal 5'-phosphate gets dissociated from the enzyme on treatment with about 1.25 M urea, SHM1
urea-induced two-step unfolding of SHM1 with the first step being dissociation of dimer into apomonomer at low denaturant concentrations followed by unfolding of the stabilized monomer at higher denaturant concentrations. The enzyme-bound pyridoxal 5'-phosphate gets dissociated from the enzyme on treatment with about 1.25 M urea, SHM2