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(6S)-tetrahydrofolate + D-serine
5,10-methylenetetrahydrofolate + glycine + H2O
(6S)-tetrahydrofolate + L-serine
5,10-methylenetetrahydrofolate + glycine + H2O
5,10-methenyl-tetrahydropteroyl pentaglutamate + glycine + H2O
5-formyl-tetrahydropteroyl pentaglutamate + L-serine
5,10-methylenetetrahydrofolate + glycine + H2O
tetrahydrofolate + D-serine
5,10-methylenetetrahydrofolate + glycine + H2O
tetrahydrofolate + L-Ser
-
the enzyme is a major source of one-carbon units for cellular metabolism. Potential for disruption of SHMT-mediated one-carbon metabolism by inadequate vitamin B-6 intake
-
-
r
5,10-methylenetetrahydrofolate + glycine + H2O
tetrahydrofolate + L-serine
5,6,7,8-tetrahydrofolate + L-Ser
5,10-methylenetetrahydrofolate + glycine + H2O
-
-
-
-
r
alpha-methylserine + tetrahydrofolate
D-alanine + 5,10-methylenetetrahydrofolate
D-alanine + (benzyloxy)acetaldehyde + H2O
(3R)-4-(benzyloxy)-3-hydroxy-L-isovaline + (3S)-4-(benzyloxy)-3-hydroxy-L-isovaline
D-alanine + 2-fluorobenzaldehyde + H2O
(2S,3S)-2-amino-3-(2-fluorophenyl)-3-hydroxy-2-methylpropanoic acid + (2S,3R)-2-amino-3-(2-fluorophenyl)-3-hydroxy-2-methylpropanoic acid
D-alanine + 3-phenylpropanal + H2O
(3S)-3-hydroxy-2-methyl-5-phenyl-L-norvaline + (3R)-3-hydroxy-2-methyl-5-phenyl-L-norvaline
D-alanine + 4-(benzyloxy)butanal + H2O
(3R)-3-hydroxy-4-(3-phenylpropoxy)-L-isovaline + (3S)-3-hydroxy-4-(3-phenylpropoxy)-L-isovaline
-
-
-
?
D-alanine + 4-chlorobenzaldehyde + H2O
(2S,3S)-2-amino-3-(4-chlorophenyl)-3-hydroxy-2-methylpropanoic acid + (2S,3R)-2-amino-3-(4-chlorophenyl)-3-hydroxy-2-methylpropanoic acid
-
-
-
?
D-alanine + 4-formylphenyl acetate + H2O
(2S,3S)-3-[4-(acetyloxy)phenyl]-2-amino-3-hydroxy-2-methylpropanoic acid + (2S,3R)-3-[4-(acetyloxy)phenyl]-2-amino-3-hydroxy-2-methylpropanoic acid
-
-
-
?
D-alanine + 4-hydroxybenzaldehyde + H2O
(2S,3S)-2-amino-3-hydroxy-3-(4-hydroxyphenyl)-2-methylpropanoic acid + (2S,3R)-2-amino-3-hydroxy-3-(4-hydroxyphenyl)-2-methylpropanoic acid
-
-
-
?
D-alanine + 4-nitrobenzaldehyde + H2O
(2S,3S)-2-amino-3-hydroxy-2-methyl-3-(4-nitrophenyl)propanoic acid + (2S,3R)-2-amino-3-hydroxy-2-methyl-3-(4-nitrophenyl)propanoic acid
-
-
-
?
D-alanine + benzaldehyde + H2O
(2S,3S)-2-amino-3-hydroxy-2-methyl-3-phenylpropanoic acid + (2S,3R)-2-amino-3-hydroxy-2-methyl-3-phenylpropanoic acid
-
-
-
?
D-alanine + benzyl (2-oxoethyl)carbamate + H2O
(3S)-4-[[(benzyloxy)carbonyl]amino]-3-hydroxy-L-isovaline + (3R)-4-[[(benzyloxy)carbonyl]amino]-3-hydroxy-L-isovaline
-
-
-
?
D-alanine + benzyl (3-oxopropyl)carbamate + H2O
(3S)-N6-[(benzyloxy)carbonyl]-3-hydroxy-2-methyl-L-lysine + (2S,3R)-2-amino-6-[[(benzyloxy)carbonyl]amino]-3-hydroxy-2-methylhexanoic acid
-
-
-
?
D-alanine + benzyl [(2R)-1-oxopropan-2-yl]carbamate + H2O
(3S)-N6-[(benzyloxy)carbonyl]-3-hydroxy-2-methyl-L-lysine + (3R)-N6-[(benzyloxy)carbonyl]-3-hydroxy-2-methyl-L-lysine
-
-
-
?
D-alanine + benzyl [(2S)-1-oxopropan-2-yl]carbamate + H2O
(3S,4S)-4-([(benzyloxy)carbonyl]amino)-3-hydroxy-2-methyl-L-norvaline + (3R,4S)-4-([(benzyloxy)carbonyl]amino)-3-hydroxy-2-methyl-L-norvaline
-
-
-
?
D-alanine + pentafluorobenzaldehyde + H2O
(2S,3S)-2-amino-3-hydroxy-2-methyl-3-(pentafluorophenyl)propanoic acid + (2S,3R)-2-amino-3-hydroxy-2-methyl-3-(pentafluorophenyl)propanoic acid
-
-
-
?
D-alanine + phenoxyacetaldehyde + H2O
(3R)-3-hydroxy-4-phenoxy-L-isovaline + (3S)-3-hydroxy-4-phenoxy-L-isovaline
-
-
-
?
D-alanine + phenylacetaldehyde + H2O
(3S)-3-hydroxy-4-phenyl-L-isovaline + (3R)-3-hydroxy-4-phenyl-L-isovaline
-
-
-
?
D-serine + (benzyloxy)acetaldehyde + H2O
(3R)-4-(benzyloxy)-2',3-dihydroxy-L-isovaline + (3S)-4-(benzyloxy)-2',3-dihydroxy-L-isovaline
-
-
-
?
D-serine + 2-fluorobenzaldehyde + H2O
(2S,3S)-2-amino-3-(2-fluorophenyl)-3-hydroxy-2-(hydroxymethyl)propanoic acid + (2S,3R)-2-amino-3-(2-fluorophenyl)-3-hydroxy-2-(hydroxymethyl)propanoic acid
-
-
-
?
D-serine + 3-phenylpropanal + H2O
(3S)-3-hydroxy-2-(hydroxymethyl)-5-phenyl-L-norvaline + (3R)-3-hydroxy-2-(hydroxymethyl)-5-phenyl-L-norvaline
-
-
-
?
D-serine + 4-(benzyloxy)butanal + H2O
(3S)-4-[[(benzyloxy)carbonyl]amino]-2',3-dihydroxy-L-isovaline + (3S)-2',3-dihydroxy-4-(3-phenylpropoxy)-L-isovaline
-
-
-
?
D-serine + 4-chlorobenzaldehyde + H2O
(2S,3S)-2-amino-3-(4-chlorophenyl)-3-hydroxy-2-(hydroxymethyl)propanoic acid + (2S,3R)-2-amino-3-(4-chlorophenyl)-3-hydroxy-2-(hydroxymethyl)propanoic acid
-
-
-
?
D-serine + 4-formylphenyl acetate + H2O
(2S,3S)-3-[4-(acetyloxy)phenyl]-2-amino-3-hydroxy-2-(hydroxymethyl)propanoic acid + (2S,3R)-3-[4-(acetyloxy)phenyl]-2-amino-3-hydroxy-2-(hydroxymethyl)propanoic acid
-
-
-
?
D-serine + 4-hydroxybenzaldehyde + H2O
(2S,3S)-2-amino-3-hydroxy-2-(hydroxymethyl)-3-(4-hydroxyphenyl)propanoic acid + (2S,3R)-2-amino-3-hydroxy-2-(hydroxymethyl)-3-(4-hydroxyphenyl)propanoic acid
-
-
-
?
D-serine + 4-nitrobenzaldehyde + H2O
(2S,3S)-2-amino-3-hydroxy-2-(hydroxymethyl)-3-(4-nitrophenyl)propanoic acid + (2S,3R)-2-amino-3-hydroxy-2-(hydroxymethyl)-3-(4-nitrophenyl)propanoic acid
-
-
-
?
D-serine + benzaldehyde + H2O
(2S,3S)-2-amino-3-hydroxy-2-(hydroxymethyl)-3-phenylpropanoic acid + (2S,3R)-2-amino-3-hydroxy-2-(hydroxymethyl)-3-phenylpropanoic acid
-
-
-
?
D-serine + benzyl (2-oxoethyl)carbamate + H2O
(3S)-4-[[(benzyloxy)carbonyl]amino]-2',3-dihydroxy-L-isovaline + (3R)-4-[[(benzyloxy)carbonyl]amino]-2',3-dihydroxy-L-isovaline
-
-
-
?
D-serine + benzyl (3-oxopropyl)carbamate + H2O
(3S)-N6-[(benzyloxy)carbonyl]-3-hydroxy-2-(hydroxymethyl)-L-lysine + (3R)-N6-[(benzyloxy)carbonyl]-3-hydroxy-2-(hydroxymethyl)-L-lysine
-
-
-
?
D-serine + benzyl [(2R)-1-oxopropan-2-yl]carbamate + H2O
(3S,4R)-4-[[(benzyloxy)carbonyl]amino]-3-hydroxy-2-(hydroxymethyl)-L-norvaline + (3R,4R)-4-[[(benzyloxy)carbonyl]amino]-3-hydroxy-2-(hydroxymethyl)-L-norvaline
-
-
-
?
D-serine + benzyl [(2S)-1-oxopropan-2-yl]carbamate + H2O
(3S,4S)-4-[[(benzyloxy)carbonyl]amino]-3-hydroxy-2-(hydroxymethyl)-L-norvaline + (3R,4S)-4-[[(benzyloxy)carbonyl]amino]-3-hydroxy-2-(hydroxymethyl)-L-norvaline
-
-
-
?
D-serine + pentafluorobenzaldehyde + H2O
(2S,3S)-2-amino-3-hydroxy-2-(hydroxymethyl)-3-(pentafluorophenyl)propanoic acid + (2S,3R)-2-amino-3-hydroxy-2-(hydroxymethyl)-3-(pentafluorophenyl)propanoic acid
-
-
-
?
D-serine + phenoxyacetaldehyde + H2O
(3R)-2',3-dihydroxy-4-phenoxy-L-isovaline + (3S)-2',3-dihydroxy-4-phenoxy-L-isovaline
-
-
-
?
D-serine + phenylacetaldehyde + H2O
(3S)-2',3-dihydroxy-4-phenyl-L-isovaline + (3R)-2',3-dihydroxy-4-phenyl-L-isovaline
-
-
-
?
D-serine + tetrahydrofolate
glycine + 5,10-methylenetetrahydrofolate + H2O
DL-3-phenylserine + ?
benzaldehyde + ?
-
-
-
?
DL-phenylserine + ?
benzaldehyde + ?
-
-
-
-
?
glycine + (benzyloxy)acetaldehyde + H2O
(2S,3R)-2-amino-4-(benzyloxy)-3-hydroxybutanoic acid + (2S,3S)-2-amino-4-(benzyloxy)-3-hydroxybutanoic acid
-
-
-
?
glycine + 2-fluorobenzaldehyde + H2O
(2S,3S)-2-amino-3-(2-fluorophenyl)-3-hydroxypropanoic acid + (2S,3R)-2-amino-3-(2-fluorophenyl)-3-hydroxypropanoic acid
-
-
-
?
glycine + 3-phenylpropanal + H2O
(3S)-3-hydroxy-5-phenyl-L-norvaline + (3R)-3-hydroxy-5-phenyl-L-norvaline
-
-
-
?
glycine + 4-(benzyloxy)butanal + H2O
(2S,3R)-2-amino-3-hydroxy-4-(3-phenylpropoxy)butanoic acid + (2S,3S)-2-amino-3-hydroxy-4-(3-phenylpropoxy)butanoic acid
-
-
-
?
glycine + 4-chlorobenzaldehyde + H2O
(2S,3S)-2-amino-3-(4-chlorophenyl)-3-hydroxypropanoic acid + (2S,3R)-2-amino-3-(4-chlorophenyl)-3-hydroxypropanoic acid
-
-
-
?
glycine + 4-formylphenyl acetate + H2O
(2S,3S)-3-[4-(acetyloxy)phenyl]-2-amino-3-hydroxypropanoic acid + (2S,3R)-3-[4-(acetyloxy)phenyl]-2-amino-3-hydroxypropanoic acid
-
-
-
?
glycine + 4-hydroxybenzaldehyde + H2O
(2S,3S)-2-amino-3-hydroxy-3-(4-hydroxyphenyl)propanoic acid + (2S,3R)-2-amino-3-hydroxy-3-(4-hydroxyphenyl)propanoic acid
-
-
-
?
glycine + 4-nitrobenzaldehyde + H2O
(2S,3S)-2-amino-3-hydroxy-3-(4-nitrophenyl)propanoic acid + (2S,3R)-2-amino-3-hydroxy-3-(4-nitrophenyl)propanoic acid
-
-
-
?
glycine + benzaldehyde + H2O
(2S,3S)-2-amino-3-hydroxy-3-phenylpropanoic acid + (2S,3R)-2-amino-3-hydroxy-3-phenylpropanoic acid
-
-
-
?
glycine + benzyl (2-oxoethyl)carbamate + H2O
(2S,3S)-2-amino-4-[[(benzyloxy)carbonyl]amino]-3-hydroxybutanoic acid + (2S,3R)-2-amino-4-[[(benzyloxy)carbonyl]amino]-3-hydroxybutanoic acid
-
-
-
?
glycine + benzyl (3-oxopropyl)carbamate + H2O
(2S,3S)-2-amino-6-[[(benzyloxy)carbonyl]amino]-3-hydroxyhexanoic acid + (2S,3R)-2-amino-6-[[(benzyloxy)carbonyl]amino]-3-hydroxyhexanoic acid
-
-
-
?
glycine + benzyl [(2R)-1-oxopropan-2-yl]carbamate + H2O
(2S,3S,4R)-2-amino-4-[[(benzyloxy)carbonyl]amino]-3-hydroxy-2-methylpentanoic acid + (2S,3S,4R)-2-amino-4-[[(benzyloxy)carbonyl]amino]-3-hydroxypentanoic acid
-
-
-
?
glycine + benzyl [(2S)-1-oxopropan-2-yl]carbamate + H2O
(2S,3R,4S)-2-amino-4-[[(benzyloxy)carbonyl]amino]-3-hydroxypentanoic acid + (2S,3S,4S)-2-amino-4-[[(benzyloxy)carbonyl]amino]-3-hydroxypentanoic acid
-
-
-
?
glycine + pentafluorobenzaldehyde + H2O
(2S,3S)-2-amino-3-hydroxy-3-(pentafluorophenyl)propanoic acid + (2S,3R)-2-amino-3-hydroxy-3-(pentafluorophenyl)propanoic acid
-
-
-
?
glycine + phenoxyacetaldehyde + H2O
(2S,3R)-2-amino-3-hydroxy-4-phenoxybutanoic acid + (2S,3S)-2-amino-3-hydroxy-4-phenoxybutanoic acid
-
-
-
?
glycine + phenylacetaldehyde + H2O
(2S,3S)-2-amino-3-hydroxy-4-phenylbutanoic acid + (2S,3R)-2-amino-3-hydroxy-4-phenylbutanoic acid
-
-
-
?
L-Ser + tetrahydrofolate
Gly + 5,10-methylenetetrahydrofolate
L-Ser + tetrahydrofolate
glycine + 5,10-methylenetetrahydrofolate + H2O
L-serine + modified folate
glycine + modified methylenefolate
L-serine + tetrahydrofolate
glycine + 5,10-methylenetetrahydrofolate + H2O
L-serine + tetrahydropteroylglutamate
glycine + 5,10-methylene-tetrahydropteroylglutamate + H2O
tetrahydrofolate + L-Ser
5,10-methylenetetrahydrofolate + glycine
tetrahydrofolate + L-Ser
? + glycine + H2O
-
-
-
-
?
tetrahydrofolate + L-serine
5,10-methylenetetrahydrofolate + glycine + H2O
tetrahydromethanopterin + L-Ser
glycine + ?
-
-
-
-
?
tetrahydropteroylglutamate + L-Ser
glycine + ?
-
-
-
-
?
additional information
?
-
(6S)-tetrahydrofolate + D-serine
5,10-methylenetetrahydrofolate + glycine + H2O
poor activity
-
-
r
(6S)-tetrahydrofolate + D-serine
5,10-methylenetetrahydrofolate + glycine + H2O
-
-
-
-
r
(6S)-tetrahydrofolate + D-serine
5,10-methylenetetrahydrofolate + glycine + H2O
-
-
-
-
r
(6S)-tetrahydrofolate + L-serine
5,10-methylenetetrahydrofolate + glycine + H2O
-
-
-
r
(6S)-tetrahydrofolate + L-serine
5,10-methylenetetrahydrofolate + glycine + H2O
the enzyme also catalyzes the formation of methylene-tetrahydromethanopterin from tetrahydromethanopterin and L-serine, albeit with a catalytic efficiency which is less than 1% of that with (6S)-tetrahydrofolate as substrate. The catalytic efficiency with methylene-tetrahydrosarcinapterin as substrate is even lower
-
-
?
(6S)-tetrahydrofolate + L-serine
5,10-methylenetetrahydrofolate + glycine + H2O
the enzyme also catalyzes the formation of methylene-tetrahydromethanopterin from tetrahydromethanopterin and L-serine, albeit with a catalytic efficiency which is less than 1% of that with (6S)-tetrahydrofolate as substrate. The catalytic efficiency with methylene-tetrahydrosarcinapterin as substrate is even lower
-
-
?
(6S)-tetrahydrofolate + L-serine
5,10-methylenetetrahydrofolate + glycine + H2O
-
-
-
-
r
(6S)-tetrahydrofolate + L-serine
5,10-methylenetetrahydrofolate + glycine + H2O
-
-
-
-
r
5,10-methenyl-tetrahydropteroyl pentaglutamate + glycine + H2O
5-formyl-tetrahydropteroyl pentaglutamate + L-serine
-
-
-
-
?
5,10-methenyl-tetrahydropteroyl pentaglutamate + glycine + H2O
5-formyl-tetrahydropteroyl pentaglutamate + L-serine
-
-
-
?
5,10-methylenetetrahydrofolate + glycine + H2O
tetrahydrofolate + D-serine
-
-
-
-
r
5,10-methylenetetrahydrofolate + glycine + H2O
tetrahydrofolate + D-serine
-
-
-
-
r
5,10-methylenetetrahydrofolate + glycine + H2O
tetrahydrofolate + D-serine
-
-
-
r
5,10-methylenetetrahydrofolate + glycine + H2O
tetrahydrofolate + L-serine
-
-
-
-
r
5,10-methylenetetrahydrofolate + glycine + H2O
tetrahydrofolate + L-serine
-
-
-
-
r
5,10-methylenetetrahydrofolate + glycine + H2O
tetrahydrofolate + L-serine
-
-
-
-
r
5,10-methylenetetrahydrofolate + glycine + H2O
tetrahydrofolate + L-serine
-
-
-
-
r
5,10-methylenetetrahydrofolate + glycine + H2O
tetrahydrofolate + L-serine
-
-
-
r
5,10-methylenetetrahydrofolate + glycine + H2O
tetrahydrofolate + L-serine
-
i.e. tetrahydropteroylglutamate, tetrahydropteroylglutamates with more than one glutamate residue are poor substrates and competitive inhibitors, overview
-
r
5,10-methylenetetrahydrofolate + glycine + H2O
tetrahydrofolate + L-serine
-
-
-
-
r
5,10-methylenetetrahydrofolate + glycine + H2O
tetrahydrofolate + L-serine
-
-
-
-
r
5,10-methylenetetrahydrofolate + glycine + H2O
tetrahydrofolate + L-serine
-
-
-
-
r
5,10-methylenetetrahydrofolate + glycine + H2O
tetrahydrofolate + L-serine
-
-
-
-
r
5,10-methylenetetrahydrofolate + glycine + H2O
tetrahydrofolate + L-serine
-
-
-
r
5,10-methylenetetrahydrofolate + glycine + H2O
tetrahydrofolate + L-serine
-
-
-
r
5,10-methylenetetrahydrofolate + glycine + H2O
tetrahydrofolate + L-serine
-
-
-
r
5,10-methylenetetrahydrofolate + glycine + H2O
tetrahydrofolate + L-serine
-
-
-
r
5,10-methylenetetrahydrofolate + glycine + H2O
tetrahydrofolate + L-serine
-
-
-
r
5,10-methylenetetrahydrofolate + glycine + H2O
tetrahydrofolate + L-serine
-
-
-
r
5,10-methylenetetrahydrofolate + glycine + H2O
tetrahydrofolate + L-serine
-
-
-
r
5,10-methylenetetrahydrofolate + glycine + H2O
tetrahydrofolate + L-serine
-
-
-
-
?
5,10-methylenetetrahydrofolate + glycine + H2O
tetrahydrofolate + L-serine
-
-
-
r
5,10-methylenetetrahydrofolate + glycine + H2O
tetrahydrofolate + L-serine
-
tetrahydrofolate-dependent SHMT activity, modeling of substrate binding, overview
-
-
?
5,10-methylenetetrahydrofolate + glycine + H2O
tetrahydrofolate + L-serine
-
-
-
r
5,10-methylenetetrahydrofolate + glycine + H2O
tetrahydrofolate + L-serine
-
-
-
-
r
5,10-methylenetetrahydrofolate + glycine + H2O
tetrahydrofolate + L-serine
-
-
-
r
5,10-methylenetetrahydrofolate + glycine + H2O
tetrahydrofolate + L-serine
-
-
-
r
5,10-methylenetetrahydrofolate + glycine + H2O
tetrahydrofolate + L-serine
-
-
-
-
r
5,10-methylenetetrahydrofolate + glycine + H2O
tetrahydrofolate + L-serine
-
-
-
r
5,10-methylenetetrahydrofolate + glycine + H2O
tetrahydrofolate + L-serine
-
-
-
r
5,10-methylenetetrahydrofolate + glycine + H2O
tetrahydrofolate + L-serine
-
-
-
r
5,10-methylenetetrahydrofolate + glycine + H2O
tetrahydrofolate + L-serine
-
-
-
r
5,10-methylenetetrahydrofolate + glycine + H2O
tetrahydrofolate + L-serine
-
-
-
r
5,10-methylenetetrahydrofolate + glycine + H2O
tetrahydrofolate + L-serine
-
-
-
r
5,10-methylenetetrahydrofolate + glycine + H2O
tetrahydrofolate + L-serine
-
-
-
-
r
5,10-methylenetetrahydrofolate + glycine + H2O
tetrahydrofolate + L-serine
-
-
-
-
r
5,10-methylenetetrahydrofolate + glycine + H2O
tetrahydrofolate + L-serine
-
-
-
-
?
5,10-methylenetetrahydrofolate + glycine + H2O
tetrahydrofolate + L-serine
-
tetrahydrofolate-dependent SHMT activity, modeling of substrate binding, overview
-
-
?
5,10-methylenetetrahydrofolate + glycine + H2O
tetrahydrofolate + L-serine
-
-
-
-
?
5,10-methylenetetrahydrofolate + glycine + H2O
tetrahydrofolate + L-serine
-
tetrahydrofolate-dependent SHMT activity, modeling of substrate binding, overview
-
-
?
5,10-methylenetetrahydrofolate + glycine + H2O
tetrahydrofolate + L-serine
-
-
-
-
r
5,10-methylenetetrahydrofolate + glycine + H2O
tetrahydrofolate + L-serine
-
-
-
r
5,10-methylenetetrahydrofolate + glycine + H2O
tetrahydrofolate + L-serine
-
-
-
r
5,10-methylenetetrahydrofolate + glycine + H2O
tetrahydrofolate + L-serine
-
-
-
r
5,10-methylenetetrahydrofolate + glycine + H2O
tetrahydrofolate + L-serine
-
-
-
r
5,10-methylenetetrahydrofolate + glycine + H2O
tetrahydrofolate + L-serine
-
-
-
r
5,10-methylenetetrahydrofolate + glycine + H2O
tetrahydrofolate + L-serine
-
-
-
r
5,10-methylenetetrahydrofolate + glycine + H2O
tetrahydrofolate + L-serine
-
-
-
r
5,10-methylenetetrahydrofolate + glycine + H2O
tetrahydrofolate + L-serine
-
-
-
-
?
5,10-methylenetetrahydrofolate + glycine + H2O
tetrahydrofolate + L-serine
-
-
-
-
r
5,10-methylenetetrahydrofolate + glycine + H2O
tetrahydrofolate + L-serine
-
tetrahydrofolate-dependent SHMT activity, modeling of substrate binding, overview
-
-
?
5,10-methylenetetrahydrofolate + glycine + H2O
tetrahydrofolate + L-serine
-
-
-
-
r
5,10-methylenetetrahydrofolate + glycine + H2O
tetrahydrofolate + L-serine
-
-
-
-
?
5,10-methylenetetrahydrofolate + glycine + H2O
tetrahydrofolate + L-serine
-
tetrahydrofolate-dependent SHMT activity, modeling of substrate binding, overview
-
-
?
5,10-methylenetetrahydrofolate + glycine + H2O
tetrahydrofolate + L-serine
-
-
-
-
r
5,10-methylenetetrahydrofolate + glycine + H2O
tetrahydrofolate + L-serine
-
-
-
-
r
5,10-methylenetetrahydrofolate + glycine + H2O
tetrahydrofolate + L-serine
-
-
-
-
r
5,10-methylenetetrahydrofolate + glycine + H2O
tetrahydrofolate + L-serine
-
-
-
-
?
5,10-methylenetetrahydrofolate + glycine + H2O
tetrahydrofolate + L-serine
-
-
-
-
r
5,10-methylenetetrahydrofolate + glycine + H2O
tetrahydrofolate + L-serine
-
-
-
-
r
5,10-methylenetetrahydrofolate + glycine + H2O
tetrahydrofolate + L-serine
-
-
-
r
5,10-methylenetetrahydrofolate + glycine + H2O
tetrahydrofolate + L-serine
-
-
-
-
r
5,10-methylenetetrahydrofolate + glycine + H2O
tetrahydrofolate + L-serine
-
-
-
r
5,10-methylenetetrahydrofolate + glycine + H2O
tetrahydrofolate + L-serine
-
-
-
r
5,10-methylenetetrahydrofolate + glycine + H2O
tetrahydrofolate + L-serine
-
-
-
r
5,10-methylenetetrahydrofolate + glycine + H2O
tetrahydrofolate + L-serine
-
-
-
r
5,10-methylenetetrahydrofolate + glycine + H2O
tetrahydrofolate + L-serine
-
-
-
-
r
5,10-methylenetetrahydrofolate + glycine + H2O
tetrahydrofolate + L-serine
-
-
-
r
5,10-methylenetetrahydrofolate + glycine + H2O
tetrahydrofolate + L-serine
-
-
-
r
5,10-methylenetetrahydrofolate + glycine + H2O
tetrahydrofolate + L-serine
-
-
-
r
5,10-methylenetetrahydrofolate + glycine + H2O
tetrahydrofolate + L-serine
-
-
-
-
r
5,10-methylenetetrahydrofolate + glycine + H2O
tetrahydrofolate + L-serine
-
-
-
-
r
5,10-methylenetetrahydrofolate + glycine + H2O
tetrahydrofolate + L-serine
-
-
-
r
5,10-methylenetetrahydrofolate + glycine + H2O
tetrahydrofolate + L-serine
-
-
-
r
5,10-methylenetetrahydrofolate + glycine + H2O
tetrahydrofolate + L-serine
-
-
-
r
5,10-methylenetetrahydrofolate + glycine + H2O
tetrahydrofolate + L-serine
-
-
-
r
5,10-methylenetetrahydrofolate + glycine + H2O
tetrahydrofolate + L-serine
-
-
-
r
5,10-methylenetetrahydrofolate + glycine + H2O
tetrahydrofolate + L-serine
-
-
-
r
5,10-methylenetetrahydrofolate + glycine + H2O
tetrahydrofolate + L-serine
-
-
-
r
alpha-methylserine + tetrahydrofolate
D-alanine + 5,10-methylenetetrahydrofolate
-
-
-
?
alpha-methylserine + tetrahydrofolate
D-alanine + 5,10-methylenetetrahydrofolate
-
-
-
?
alpha-methylserine + tetrahydrofolate
D-alanine + 5,10-methylenetetrahydrofolate
-
-
-
?
alpha-methylserine + tetrahydrofolate
D-alanine + 5,10-methylenetetrahydrofolate
-
-
-
-
?
alpha-methylserine + tetrahydrofolate
D-alanine + 5,10-methylenetetrahydrofolate
-
-
-
-
?
alpha-methylserine + tetrahydrofolate
D-alanine + 5,10-methylenetetrahydrofolate
-
-
-
?
alpha-methylserine + tetrahydrofolate
D-alanine + 5,10-methylenetetrahydrofolate
-
-
-
?
alpha-methylserine + tetrahydrofolate
D-alanine + 5,10-methylenetetrahydrofolate
-
-
-
?
alpha-methylserine + tetrahydrofolate
D-alanine + 5,10-methylenetetrahydrofolate
-
-
-
?
alpha-methylserine + tetrahydrofolate
D-alanine + 5,10-methylenetetrahydrofolate
-
-
-
?
alpha-methylserine + tetrahydrofolate
D-alanine + 5,10-methylenetetrahydrofolate
-
at high concentrations of enzyme
-
?
alpha-methylserine + tetrahydrofolate
D-alanine + 5,10-methylenetetrahydrofolate
-
-
-
?
alpha-methylserine + tetrahydrofolate
D-alanine + 5,10-methylenetetrahydrofolate
-
-
-
?
alpha-methylserine + tetrahydrofolate
D-alanine + 5,10-methylenetetrahydrofolate
-
-
-
?
alpha-methylserine + tetrahydrofolate
D-alanine + 5,10-methylenetetrahydrofolate
-
-
-
-
?
alpha-methylserine + tetrahydrofolate
D-alanine + 5,10-methylenetetrahydrofolate
-
-
-
-
?
alpha-methylserine + tetrahydrofolate
D-alanine + 5,10-methylenetetrahydrofolate
-
-
-
?
D-alanine + (benzyloxy)acetaldehyde + H2O
(3R)-4-(benzyloxy)-3-hydroxy-L-isovaline + (3S)-4-(benzyloxy)-3-hydroxy-L-isovaline
-
-
-
?
D-alanine + (benzyloxy)acetaldehyde + H2O
(3R)-4-(benzyloxy)-3-hydroxy-L-isovaline + (3S)-4-(benzyloxy)-3-hydroxy-L-isovaline
-
-
-
?
D-alanine + 2-fluorobenzaldehyde + H2O
(2S,3S)-2-amino-3-(2-fluorophenyl)-3-hydroxy-2-methylpropanoic acid + (2S,3R)-2-amino-3-(2-fluorophenyl)-3-hydroxy-2-methylpropanoic acid
-
-
-
?
D-alanine + 2-fluorobenzaldehyde + H2O
(2S,3S)-2-amino-3-(2-fluorophenyl)-3-hydroxy-2-methylpropanoic acid + (2S,3R)-2-amino-3-(2-fluorophenyl)-3-hydroxy-2-methylpropanoic acid
-
-
-
?
D-alanine + 3-phenylpropanal + H2O
(3S)-3-hydroxy-2-methyl-5-phenyl-L-norvaline + (3R)-3-hydroxy-2-methyl-5-phenyl-L-norvaline
-
-
-
?
D-alanine + 3-phenylpropanal + H2O
(3S)-3-hydroxy-2-methyl-5-phenyl-L-norvaline + (3R)-3-hydroxy-2-methyl-5-phenyl-L-norvaline
-
-
-
?
D-serine + tetrahydrofolate
glycine + 5,10-methylenetetrahydrofolate + H2O
-
the catalytic efficiency for D-serine is 580fold lower than that of L-serine
-
-
?
D-serine + tetrahydrofolate
glycine + 5,10-methylenetetrahydrofolate + H2O
-
the catalytic efficiency for D-serine is 580fold lower than that of L-serine
-
-
?
D-serine + tetrahydrofolate
glycine + 5,10-methylenetetrahydrofolate + H2O
-
the binding affinity for D-serine is 150fold lower than that of L-serine
-
-
?
L-Ser + tetrahydrofolate
Gly + 5,10-methylenetetrahydrofolate
-
-
-
-
r
L-Ser + tetrahydrofolate
Gly + 5,10-methylenetetrahydrofolate
-
-
-
-
?
L-Ser + tetrahydrofolate
Gly + 5,10-methylenetetrahydrofolate
-
-
-
-
r
L-Ser + tetrahydrofolate
Gly + 5,10-methylenetetrahydrofolate
-
-
-
?
L-Ser + tetrahydrofolate
Gly + 5,10-methylenetetrahydrofolate
-
-
-
-
?
L-Ser + tetrahydrofolate
Gly + 5,10-methylenetetrahydrofolate
-
placental conversion of serine to glycine is a major source of fetal glycine
-
-
?
L-Ser + tetrahydrofolate
glycine + 5,10-methylenetetrahydrofolate + H2O
-
-
-
-
?
L-Ser + tetrahydrofolate
glycine + 5,10-methylenetetrahydrofolate + H2O
-
-
-
-
?
L-Ser + tetrahydrofolate
glycine + 5,10-methylenetetrahydrofolate + H2O
-
-
-
-
?
L-Ser + tetrahydrofolate
glycine + 5,10-methylenetetrahydrofolate + H2O
-
-
-
-
?
L-Ser + tetrahydrofolate
glycine + 5,10-methylenetetrahydrofolate + H2O
-
-
-
-
?
L-Ser + tetrahydrofolate
glycine + 5,10-methylenetetrahydrofolate + H2O
-
-
-
-
?
L-Ser + tetrahydrofolate
glycine + 5,10-methylenetetrahydrofolate + H2O
-
-
-
-
?
L-Ser + tetrahydrofolate
glycine + 5,10-methylenetetrahydrofolate + H2O
-
-
-
-
?
L-Ser + tetrahydrofolate
glycine + 5,10-methylenetetrahydrofolate + H2O
-
-
-
-
?
L-Ser + tetrahydrofolate
glycine + 5,10-methylenetetrahydrofolate + H2O
-
-
-
-
?
L-serine + modified folate
glycine + modified methylenefolate
not: tetrahydrofolate, synthetic modified folate derivate
-
?
L-serine + modified folate
glycine + modified methylenefolate
not: tetrahydrofolate, synthetic modified folate derivate
-
?
L-serine + tetrahydrofolate
glycine + 5,10-methylenetetrahydrofolate + H2O
-
-
-
-
?
L-serine + tetrahydrofolate
glycine + 5,10-methylenetetrahydrofolate + H2O
-
-
-
-
?
L-serine + tetrahydrofolate
glycine + 5,10-methylenetetrahydrofolate + H2O
-
-
-
-
?
L-serine + tetrahydrofolate
glycine + 5,10-methylenetetrahydrofolate + H2O
-
-
-
?
L-serine + tetrahydrofolate
glycine + 5,10-methylenetetrahydrofolate + H2O
-
may play important role in central nervous system
-
?
L-serine + tetrahydrofolate
glycine + 5,10-methylenetetrahydrofolate + H2O
-
-
-
-
?
L-serine + tetrahydrofolate
glycine + 5,10-methylenetetrahydrofolate + H2O
-
-
-
-
?
L-serine + tetrahydrofolate
glycine + 5,10-methylenetetrahydrofolate + H2O
-
-
-
?
L-serine + tetrahydrofolate
glycine + 5,10-methylenetetrahydrofolate + H2O
-
-
-
?
L-serine + tetrahydrofolate
glycine + 5,10-methylenetetrahydrofolate + H2O
-
may play important role in central nervous system
-
?
L-serine + tetrahydrofolate
glycine + 5,10-methylenetetrahydrofolate + H2O
-
-
-
?
L-serine + tetrahydrofolate
glycine + 5,10-methylenetetrahydrofolate + H2O
-
-
-
?
L-serine + tetrahydrofolate
glycine + 5,10-methylenetetrahydrofolate + H2O
-
-
-
-
?
L-serine + tetrahydrofolate
glycine + 5,10-methylenetetrahydrofolate + H2O
-
-
-
?
L-serine + tetrahydrofolate
glycine + 5,10-methylenetetrahydrofolate + H2O
-
-
-
-
r
L-serine + tetrahydrofolate
glycine + 5,10-methylenetetrahydrofolate + H2O
-
-
-
r
L-serine + tetrahydrofolate
glycine + 5,10-methylenetetrahydrofolate + H2O
-
-
-
?
L-serine + tetrahydrofolate
glycine + 5,10-methylenetetrahydrofolate + H2O
-
-
-
-
?
L-serine + tetrahydrofolate
glycine + 5,10-methylenetetrahydrofolate + H2O
-
-
-
r
L-serine + tetrahydrofolate
glycine + 5,10-methylenetetrahydrofolate + H2O
-
major pathway for production of C1-units of 5,10-methylenetetrahydrofolate
-
?
L-serine + tetrahydrofolate
glycine + 5,10-methylenetetrahydrofolate + H2O
-
major pathway for production of C1-units of 5,10-methylenetetrahydrofolate
-
?
L-serine + tetrahydrofolate
glycine + 5,10-methylenetetrahydrofolate + H2O
-
catalyzes interconversion of serine and glycine
-
?
L-serine + tetrahydrofolate
glycine + 5,10-methylenetetrahydrofolate + H2O
-
enzyme plays a pivotal role in channelling metabolites between amino acid and nucleotide metabolism
-
?
L-serine + tetrahydrofolate
glycine + 5,10-methylenetetrahydrofolate + H2O
-
-
-
?
L-serine + tetrahydrofolate
glycine + 5,10-methylenetetrahydrofolate + H2O
-
-
-
r
L-serine + tetrahydrofolate
glycine + 5,10-methylenetetrahydrofolate + H2O
-
-
-
r
L-serine + tetrahydrofolate
glycine + 5,10-methylenetetrahydrofolate + H2O
-
-
-
?
L-serine + tetrahydrofolate
glycine + 5,10-methylenetetrahydrofolate + H2O
-
-
-
?
L-serine + tetrahydrofolate
glycine + 5,10-methylenetetrahydrofolate + H2O
-
-
-
?
L-serine + tetrahydrofolate
glycine + 5,10-methylenetetrahydrofolate + H2O
-
-
-
-
?
L-serine + tetrahydrofolate
glycine + 5,10-methylenetetrahydrofolate + H2O
-
-
-
r
L-serine + tetrahydrofolate
glycine + 5,10-methylenetetrahydrofolate + H2O
-
-
-
?
L-serine + tetrahydrofolate
glycine + 5,10-methylenetetrahydrofolate + H2O
-
-
-
r
L-serine + tetrahydrofolate
glycine + 5,10-methylenetetrahydrofolate + H2O
-
main glycine source for purine biosynthetic pathway in ureide biogenesis
-
?
L-serine + tetrahydrofolate
glycine + 5,10-methylenetetrahydrofolate + H2O
-
-
-
r
L-serine + tetrahydrofolate
glycine + 5,10-methylenetetrahydrofolate + H2O
-
main glycine source for purine biosynthetic pathway in ureide biogenesis
-
?
L-serine + tetrahydrofolate
glycine + 5,10-methylenetetrahydrofolate + H2O
-
-
-
?
L-serine + tetrahydrofolate
glycine + 5,10-methylenetetrahydrofolate + H2O
-
-
-
?
L-serine + tetrahydrofolate
glycine + 5,10-methylenetetrahydrofolate + H2O
-
-
-
-
?
L-serine + tetrahydrofolate
glycine + 5,10-methylenetetrahydrofolate + H2O
-
-
-
-
r
L-serine + tetrahydrofolate
glycine + 5,10-methylenetetrahydrofolate + H2O
-
-
-
r
L-serine + tetrahydrofolate
glycine + 5,10-methylenetetrahydrofolate + H2O
-
-
-
r
L-serine + tetrahydrofolate
glycine + 5,10-methylenetetrahydrofolate + H2O
-
major pathway for production of C1-units of 5,10-methylenetetrahydrofolate
-
?
L-serine + tetrahydrofolate
glycine + 5,10-methylenetetrahydrofolate + H2O
-
major pathway for production of C1-units of 5,10-methylenetetrahydrofolate
-
?
L-serine + tetrahydrofolate
glycine + 5,10-methylenetetrahydrofolate + H2O
-
main glycine source for purine biosynthetic pathway in ureide biogenesis
-
?
L-serine + tetrahydrofolate
glycine + 5,10-methylenetetrahydrofolate + H2O
-
enzyme plays a pivotal role in channelling metabolites between amino acid and nucleotide metabolism
-
?
L-serine + tetrahydrofolate
glycine + 5,10-methylenetetrahydrofolate + H2O
-
-
-
r
L-serine + tetrahydrofolate
glycine + 5,10-methylenetetrahydrofolate + H2O
-
-
-
r
L-serine + tetrahydrofolate
glycine + 5,10-methylenetetrahydrofolate + H2O
-
key enzyme of serine pathway for assimilation of C1-compounds
-
?
L-serine + tetrahydrofolate
glycine + 5,10-methylenetetrahydrofolate + H2O
-
key enzyme of serine pathway for assimilation of C1-compounds
-
?
L-serine + tetrahydrofolate
glycine + 5,10-methylenetetrahydrofolate + H2O
-
-
-
?
L-serine + tetrahydrofolate
glycine + 5,10-methylenetetrahydrofolate + H2O
-
-
-
?
L-serine + tetrahydrofolate
glycine + 5,10-methylenetetrahydrofolate + H2O
-
adding 2fold more glycine in the medium increases significantly the expression of SHMT-S and to an even higher level, the expression of SHMT-L, adding 2fold more serine has the reverse effect on the expression of SHMT-L, while the expression of SHMT-S does not change significantly
-
-
?
L-serine + tetrahydrofolate
glycine + 5,10-methylenetetrahydrofolate + H2O
-
-
-
-
?
L-serine + tetrahydrofolate
glycine + 5,10-methylenetetrahydrofolate + H2O
-
-
-
-
r
L-serine + tetrahydrofolate
glycine + 5,10-methylenetetrahydrofolate + H2O
-
regulatory protein
-
?
L-serine + tetrahydrofolate
glycine + 5,10-methylenetetrahydrofolate + H2O
-
-
-
?
L-serine + tetrahydrofolate
glycine + 5,10-methylenetetrahydrofolate + H2O
-
-
-
-
r
L-serine + tetrahydrofolate
glycine + 5,10-methylenetetrahydrofolate + H2O
-
main glycine source for purine biosynthetic pathway in ureide biogenesis
-
?
L-serine + tetrahydrofolate
glycine + 5,10-methylenetetrahydrofolate + H2O
-
key enzyme of serine pathway for assimilation of C1-compounds
-
?
L-serine + tetrahydrofolate
glycine + 5,10-methylenetetrahydrofolate + H2O
-
-
-
?
L-serine + tetrahydrofolate
glycine + 5,10-methylenetetrahydrofolate + H2O
-
-
-
?
L-serine + tetrahydrofolate
glycine + 5,10-methylenetetrahydrofolate + H2O
-
may play important role in central nervous system
-
?
L-serine + tetrahydrofolate
glycine + 5,10-methylenetetrahydrofolate + H2O
-
-
-
?
L-serine + tetrahydrofolate
glycine + 5,10-methylenetetrahydrofolate + H2O
-
-
-
?
L-serine + tetrahydrofolate
glycine + 5,10-methylenetetrahydrofolate + H2O
-
-
-
-
?
L-serine + tetrahydrofolate
glycine + 5,10-methylenetetrahydrofolate + H2O
-
-
-
?
L-serine + tetrahydrofolate
glycine + 5,10-methylenetetrahydrofolate + H2O
-
-
-
r
L-serine + tetrahydrofolate
glycine + 5,10-methylenetetrahydrofolate + H2O
-
-
-
r
L-serine + tetrahydrofolate
glycine + 5,10-methylenetetrahydrofolate + H2O
-
-
-
-
r
L-serine + tetrahydrofolate
glycine + 5,10-methylenetetrahydrofolate + H2O
-
-
-
r
L-serine + tetrahydrofolate
glycine + 5,10-methylenetetrahydrofolate + H2O
-
-
-
r
L-serine + tetrahydrofolate
glycine + 5,10-methylenetetrahydrofolate + H2O
-
-
-
r
L-serine + tetrahydrofolate
glycine + 5,10-methylenetetrahydrofolate + H2O
-
-
-
-
r
L-serine + tetrahydrofolate
glycine + 5,10-methylenetetrahydrofolate + H2O
-
-
-
r
L-serine + tetrahydrofolate
glycine + 5,10-methylenetetrahydrofolate + H2O
-
-
-
?
L-serine + tetrahydrofolate
glycine + 5,10-methylenetetrahydrofolate + H2O
-
enzyme is a component of thymidylate cycle
-
?
L-serine + tetrahydrofolate
glycine + 5,10-methylenetetrahydrofolate + H2O
-
may play important role in central nervous system
-
?
L-serine + tetrahydrofolate
glycine + 5,10-methylenetetrahydrofolate + H2O
-
catalyzes interconversion of serine and glycine
-
?
L-serine + tetrahydrofolate
glycine + 5,10-methylenetetrahydrofolate + H2O
-
enzyme plays a pivotal role in channelling metabolites between amino acid and nucleotide metabolism
-
?
L-serine + tetrahydrofolate
glycine + 5,10-methylenetetrahydrofolate + H2O
-
-
-
-
?
L-serine + tetrahydrofolate
glycine + 5,10-methylenetetrahydrofolate + H2O
-
-
-
?
L-serine + tetrahydrofolate
glycine + 5,10-methylenetetrahydrofolate + H2O
-
-
-
?
L-serine + tetrahydrofolate
glycine + 5,10-methylenetetrahydrofolate + H2O
-
-
-
?
L-serine + tetrahydrofolate
glycine + 5,10-methylenetetrahydrofolate + H2O
-
-
-
?
L-serine + tetrahydrofolate
glycine + 5,10-methylenetetrahydrofolate + H2O
-
-
-
r
L-serine + tetrahydrofolate
glycine + 5,10-methylenetetrahydrofolate + H2O
-
-
-
-
r
L-serine + tetrahydrofolate
glycine + 5,10-methylenetetrahydrofolate + H2O
-
-
-
r
L-serine + tetrahydrofolate
glycine + 5,10-methylenetetrahydrofolate + H2O
-
enzyme is a component of thymidylate cycle
-
?
L-serine + tetrahydrofolate
glycine + 5,10-methylenetetrahydrofolate + H2O
-
may play important role in central nervous system
-
?
L-serine + tetrahydrofolate
glycine + 5,10-methylenetetrahydrofolate + H2O
-
enzyme plays a pivotal role in channelling metabolites between amino acid and nucleotide metabolism
-
?
L-serine + tetrahydrofolate
glycine + 5,10-methylenetetrahydrofolate + H2O
-
-
-
-
?
L-serine + tetrahydrofolate
glycine + 5,10-methylenetetrahydrofolate + H2O
-
-
-
?
L-serine + tetrahydrofolate
glycine + 5,10-methylenetetrahydrofolate + H2O
-
-
-
r
L-serine + tetrahydrofolate
glycine + 5,10-methylenetetrahydrofolate + H2O
-
enzyme plays a pivotal role in channelling metabolites between amino acid and nucleotide metabolism
-
?
L-serine + tetrahydrofolate
glycine + 5,10-methylenetetrahydrofolate + H2O
-
-
-
-
?
L-serine + tetrahydrofolate
glycine + 5,10-methylenetetrahydrofolate + H2O
-
only (6S)-tetrahydrofolate can serve as a substrate for His6-tagged SHMT, the presence of (6R)-tetrahydrofolate has no interference to the reaction
-
-
?
L-serine + tetrahydrofolate
glycine + 5,10-methylenetetrahydrofolate + H2O
-
only (6S)-tetrahydrofolate can serve as a substrate for His6-tagged SHMT, the presence of (6R)-tetrahydrofolate has no interference to the reaction
-
-
?
L-serine + tetrahydrofolate
glycine + 5,10-methylenetetrahydrofolate + H2O
-
L-serine is the physiological substrate
-
-
?
L-serine + tetrahydrofolate
glycine + 5,10-methylenetetrahydrofolate + H2O
-
-
-
-
?
L-serine + tetrahydrofolate
glycine + 5,10-methylenetetrahydrofolate + H2O
-
-
-
-
r
L-serine + tetrahydrofolate
glycine + 5,10-methylenetetrahydrofolate + H2O
-
major pathway for production of C1-units of 5,10-methylenetetrahydrofolate
-
?
L-serine + tetrahydrofolate
glycine + 5,10-methylenetetrahydrofolate + H2O
-
major pathway for production of C1-units of 5,10-methylenetetrahydrofolate
-
?
L-serine + tetrahydrofolate
glycine + 5,10-methylenetetrahydrofolate + H2O
-
catalyzes interconversion of serine and glycine
-
?
L-serine + tetrahydrofolate
glycine + 5,10-methylenetetrahydrofolate + H2O
key enzyme of serine pathway for assimilation of C1-compounds
-
?
L-serine + tetrahydrofolate
glycine + 5,10-methylenetetrahydrofolate + H2O
key enzyme of serine pathway for assimilation of C1-compounds
-
?
L-serine + tetrahydrofolate
glycine + 5,10-methylenetetrahydrofolate + H2O
-
-
-
-
?
L-serine + tetrahydrofolate
glycine + 5,10-methylenetetrahydrofolate + H2O
-
-
-
?
L-serine + tetrahydrofolate
glycine + 5,10-methylenetetrahydrofolate + H2O
-
-
-
?
L-serine + tetrahydrofolate
glycine + 5,10-methylenetetrahydrofolate + H2O
-
key enzyme of serine pathway for assimilation of C1-compounds
-
?
L-serine + tetrahydrofolate
glycine + 5,10-methylenetetrahydrofolate + H2O
-
enzyme plays a pivotal role in channelling metabolites between amino acid and nucleotide metabolism
-
?
L-serine + tetrahydrofolate
glycine + 5,10-methylenetetrahydrofolate + H2O
-
-
-
-
?
L-serine + tetrahydrofolate
glycine + 5,10-methylenetetrahydrofolate + H2O
-
key enzyme of serine pathway for assimilation of C1-compounds
-
?
L-serine + tetrahydrofolate
glycine + 5,10-methylenetetrahydrofolate + H2O
-
-
-
?
L-serine + tetrahydrofolate
glycine + 5,10-methylenetetrahydrofolate + H2O
-
may play important role in central nervous system
-
?
L-serine + tetrahydrofolate
glycine + 5,10-methylenetetrahydrofolate + H2O
-
SHMT antisense plants display lower photosynthetic capacity and accumulate glycine in light, glycine is converted to serine in the second half of the light period, serine shows an inverse diurnal rhythm and reaches highest values in darkness, glycine/serine conversion is independent of light in the transformant, but not in the wild-type
-
-
?
L-serine + tetrahydrofolate
glycine + 5,10-methylenetetrahydrofolate + H2O
-
-
-
-
?
L-serine + tetrahydrofolate
glycine + 5,10-methylenetetrahydrofolate + H2O
-
-
-
-
?
L-serine + tetrahydrofolate
glycine + 5,10-methylenetetrahydrofolate + H2O
-
-
-
-
?
L-serine + tetrahydrofolate
glycine + 5,10-methylenetetrahydrofolate + H2O
-
-
-
?
L-serine + tetrahydrofolate
glycine + 5,10-methylenetetrahydrofolate + H2O
-
-
-
r
L-serine + tetrahydrofolate
glycine + 5,10-methylenetetrahydrofolate + H2O
-
regulatory protein
-
?
L-serine + tetrahydrofolate
glycine + 5,10-methylenetetrahydrofolate + H2O
-
key enzyme of serine pathway for assimilation of C1-compounds
-
?
L-serine + tetrahydropteroylglutamate
glycine + 5,10-methylene-tetrahydropteroylglutamate + H2O
-
-
-
-
r
L-serine + tetrahydropteroylglutamate
glycine + 5,10-methylene-tetrahydropteroylglutamate + H2O
-
-
-
-
r
NADH + coenzyme Q10
?
-
-
-
?
NADH + coenzyme Q10
?
-
-
-
?
tetrahydrofolate + L-Ser
5,10-methylenetetrahydrofolate + glycine
-
-
-
r
tetrahydrofolate + L-Ser
5,10-methylenetetrahydrofolate + glycine
-
-
-
r
tetrahydrofolate + L-serine
5,10-methylenetetrahydrofolate + glycine + H2O
-
-
-
-
r
tetrahydrofolate + L-serine
5,10-methylenetetrahydrofolate + glycine + H2O
-
-
-
-
r
tetrahydrofolate + L-serine
5,10-methylenetetrahydrofolate + glycine + H2O
-
-
-
-
r
tetrahydrofolate + L-serine
5,10-methylenetetrahydrofolate + glycine + H2O
-
-
-
-
r
tetrahydrofolate + L-serine
5,10-methylenetetrahydrofolate + glycine + H2O
-
-
-
-
r
tetrahydrofolate + L-serine
5,10-methylenetetrahydrofolate + glycine + H2O
-
-
-
-
r
tetrahydrofolate + L-serine
5,10-methylenetetrahydrofolate + glycine + H2O
-
-
-
-
r
tetrahydrofolate + L-serine
5,10-methylenetetrahydrofolate + glycine + H2O
-
-
-
r
tetrahydrofolate + L-serine
5,10-methylenetetrahydrofolate + glycine + H2O
-
-
-
r
tetrahydrofolate + L-serine
5,10-methylenetetrahydrofolate + glycine + H2O
-
-
-
r
tetrahydrofolate + L-serine
5,10-methylenetetrahydrofolate + glycine + H2O
-
-
-
-
r
tetrahydrofolate + L-serine
5,10-methylenetetrahydrofolate + glycine + H2O
-
-
-
r
tetrahydrofolate + L-serine
5,10-methylenetetrahydrofolate + glycine + H2O
-
-
-
r
tetrahydrofolate + L-serine
5,10-methylenetetrahydrofolate + glycine + H2O
-
-
-
-
r
tetrahydrofolate + L-serine
5,10-methylenetetrahydrofolate + glycine + H2O
-
-
-
r
tetrahydrofolate + L-serine
5,10-methylenetetrahydrofolate + glycine + H2O
-
-
-
r
tetrahydrofolate + L-serine
5,10-methylenetetrahydrofolate + glycine + H2O
-
-
-
r
tetrahydrofolate + L-serine
5,10-methylenetetrahydrofolate + glycine + H2O
-
-
-
r
tetrahydrofolate + L-serine
5,10-methylenetetrahydrofolate + glycine + H2O
-
-
-
r
tetrahydrofolate + L-serine
5,10-methylenetetrahydrofolate + glycine + H2O
-
-
-
-
r
tetrahydrofolate + L-serine
5,10-methylenetetrahydrofolate + glycine + H2O
-
-
-
r
tetrahydrofolate + L-serine
5,10-methylenetetrahydrofolate + glycine + H2O
-
-
-
r
tetrahydrofolate + L-serine
5,10-methylenetetrahydrofolate + glycine + H2O
-
-
-
r
tetrahydrofolate + L-serine
5,10-methylenetetrahydrofolate + glycine + H2O
-
-
-
-
?
tetrahydrofolate + L-serine
5,10-methylenetetrahydrofolate + glycine + H2O
-
-
-
?
tetrahydrofolate + L-serine
5,10-methylenetetrahydrofolate + glycine + H2O
-
-
-
?
tetrahydrofolate + L-serine
5,10-methylenetetrahydrofolate + glycine + H2O
-
-
-
-
?
tetrahydrofolate + L-serine
5,10-methylenetetrahydrofolate + glycine + H2O
-
-
-
-
?
tetrahydrofolate + L-serine
5,10-methylenetetrahydrofolate + glycine + H2O
-
-
-
-
?
tetrahydrofolate + L-serine
5,10-methylenetetrahydrofolate + glycine + H2O
-
-
-
-
r
tetrahydrofolate + L-serine
5,10-methylenetetrahydrofolate + glycine + H2O
-
-
-
-
r
tetrahydrofolate + L-serine
5,10-methylenetetrahydrofolate + glycine + H2O
-
-
-
-
r
tetrahydrofolate + L-serine
5,10-methylenetetrahydrofolate + glycine + H2O
-
-
-
-
r
tetrahydrofolate + L-serine
5,10-methylenetetrahydrofolate + glycine + H2O
-
-
-
r
tetrahydrofolate + L-serine
5,10-methylenetetrahydrofolate + glycine + H2O
-
-
-
r
tetrahydrofolate + L-serine
5,10-methylenetetrahydrofolate + glycine + H2O
-
-
-
r
tetrahydrofolate + L-serine
5,10-methylenetetrahydrofolate + glycine + H2O
-
-
-
r
tetrahydrofolate + L-serine
5,10-methylenetetrahydrofolate + glycine + H2O
-
-
-
r
tetrahydrofolate + L-serine
5,10-methylenetetrahydrofolate + glycine + H2O
-
-
-
r
tetrahydrofolate + L-serine
5,10-methylenetetrahydrofolate + glycine + H2O
-
-
-
-
r
tetrahydrofolate + L-serine
5,10-methylenetetrahydrofolate + glycine + H2O
-
-
-
-
r
tetrahydrofolate + L-serine
5,10-methylenetetrahydrofolate + glycine + H2O
-
-
-
r
tetrahydrofolate + L-serine
5,10-methylenetetrahydrofolate + glycine + H2O
-
-
-
r
tetrahydrofolate + L-serine
5,10-methylenetetrahydrofolate + glycine + H2O
-
-
-
r
additional information
?
-
-
the enzyme is also active with DL-threo-3-phenylserine
-
-
?
additional information
?
-
purified recombinant ApSHMT protein exhibits catalytic reactions for DL-threo-3-phenylserine as well as for L-serine
-
-
?
additional information
?
-
-
purified recombinant ApSHMT protein exhibits catalytic reactions for DL-threo-3-phenylserine as well as for L-serine
-
-
?
additional information
?
-
-
SHMT1 functions in the photorespiratory pathway and plays a critical role in controlling the cell damage provoked by abiotic stresses such as high light and salt and in restricting pathogen induced cell death
-
-
?
additional information
?
-
-
SHMT1 functions in the photorespiratory pathway and plays a critical role in controlling the cell damage provoked by abiotic stresses such as high light and salt and in restricting pathogen induced cell death
-
-
?
additional information
?
-
-
SHMT also catalyzes the hydrolysis of 5,10-methenyl-tetrahydropteroylglutamate to 5-formyl-tetrahydropteroylglutamate
-
-
?
additional information
?
-
-
broad substrate and reaction specificity
-
-
?
additional information
?
-
-
no: L-threonine
-
-
?
additional information
?
-
-
no: D-serine
-
-
?
additional information
?
-
-
enzyme transaminates D-alanine to pyruvate and pyridoxamine phosphate
-
-
?
additional information
?
-
-
no: L-threonine
-
-
?
additional information
?
-
-
no: D-serine
-
-
?
additional information
?
-
-
review and comparison of enzyme activity, threonine aldolase and allothreonine aldolase activity from various sources
-
-
?
additional information
?
-
-
enzyme transaminates D-alanine to pyruvate and pyridoxamine phosphate
-
-
?
additional information
?
-
-
enzyme transaminates D-alanine to pyruvate and pyridoxamine phosphate
-
-
?
additional information
?
-
disruption of the SHM2 gene, encoding one of two serine hydroxymethyltransferase isoenzymes, reduces the flux from glycine to serine
-
-
?
additional information
?
-
-
disruption of the SHM2 gene, encoding one of two serine hydroxymethyltransferase isoenzymes, reduces the flux from glycine to serine
-
-
?
additional information
?
-
enzyme catalyzes the pyridoxal 5'-phosphate dependent reversible cleavage of 3-hydroxy-alpha-amino acids
-
-
?
additional information
?
-
-
enzyme catalyzes the pyridoxal 5'-phosphate dependent reversible cleavage of 3-hydroxy-alpha-amino acids
-
-
?
additional information
?
-
-
review and comparison of enzyme activity, threonine aldolase and allothreonine aldolase activity from various sources
-
-
?
additional information
?
-
-
enzyme transaminates D-alanine to pyruvate and pyridoxamine phosphate
-
-
?
additional information
?
-
-
enzyme transaminates D-alanine to pyruvate and pyridoxamine phosphate
-
-
?
additional information
?
-
-
enzyme transaminates D-alanine to pyruvate and pyridoxamine phosphate
-
-
?
additional information
?
-
enzyme transaminates D-alanine to pyruvate and pyridoxamine phosphate
-
-
?
additional information
?
-
-
enzyme transaminates D-alanine to pyruvate and pyridoxamine phosphate
-
-
?
additional information
?
-
enzyme catalyses the racemization of D- and L-alanine
-
-
?
additional information
?
-
-
enzyme catalyses the racemization of D- and L-alanine
-
-
?
additional information
?
-
-
3-phenylserine is used as a substrate
-
-
?
additional information
?
-
-
SHMT also catalyzes the hydrolysis of 5,10-methenyl-tetrahydropteroylglutamate to 5-formyl-tetrahydropteroylglutamate
-
-
?
additional information
?
-
-
broad substrate and reaction specificity, overview
-
-
?
additional information
?
-
-
SHMT activity with beta-phenylserine as substrate is about 1.48fold and 1.25fold higher than that with beta-(methylsulfonylphenyl) serine and beta-(nitrophenyl) serine as substrate, respectively. Besides SHMT activity, the enzyme also shows L-allo-threonine aldolase activity, EC 4.1.2.48
-
-
?
additional information
?
-
-
SHMT activity with beta-phenylserine as substrate is about 1.48fold and 1.25fold higher than that with beta-(methylsulfonylphenyl) serine and beta-(nitrophenyl) serine as substrate, respectively. Besides SHMT activity, the enzyme also shows L-allo-threonine aldolase activity, EC 4.1.2.48
-
-
?
additional information
?
-
-
no: D-serine
-
-
?
additional information
?
-
-
no: D-serine
-
-
?
additional information
?
-
-
no: D-allothreonine
-
-
?
additional information
?
-
-
no: D-allothreonine
-
-
?
additional information
?
-
-
no: D-threonine
-
-
?
additional information
?
-
-
no: D-threonine
-
-
?
additional information
?
-
-
no: D-serine
-
-
?
additional information
?
-
-
no: D-allothreonine
-
-
?
additional information
?
-
-
no: D-threonine
-
-
?
additional information
?
-
-
no: D-serine
-
-
?
additional information
?
-
-
no: D-allothreonine
-
-
?
additional information
?
-
-
no: D-threonine
-
-
?
additional information
?
-
-
enzyme catalyses the racemization of D- and L-alanine
-
-
?
additional information
?
-
-
enzyme catalyses the racemization of D- and L-alanine
-
-
?
additional information
?
-
SHMT also catalyses several tetrahydrofolate-independent side reactions such as cleavage of beta-hydroxy amino acids, transamination, racemization and decarboxylation
-
-
?
additional information
?
-
-
SHMT also catalyses several tetrahydrofolate-independent side reactions such as cleavage of beta-hydroxy amino acids, transamination, racemization and decarboxylation
-
-
?
additional information
?
-
-
the enzyme also exhibits tetrahydrofolate-independent aldolase activity, EC 4.1.2.5, toward beta-hydroxyamino acids, producing glycine and aldehydes
-
-
?
additional information
?
-
-
-
-
-
?
additional information
?
-
-
-
-
-
?
additional information
?
-
-
review and comparison of enzyme activity, threonine aldolase and allothreonine aldolase activity from various sources
-
-
?
additional information
?
-
-
low activity in placenta suggests that placental conversion of serine to glycine is not a major source of fetal glycine
-
-
?
additional information
?
-
-
the enzyme plays an indispensable role in nucleic acid biosynthesis
-
-
?
additional information
?
-
-
human serine hydroxymethyltransferase 2 binds specifically to heterogeneous nuclear ribonucleoprotein D
-
-
?
additional information
?
-
-
the enzyme also exhibits tetrahydrofolate-independent aldolase activity, EC 4.1.2.5, toward beta-hydroxyamino acids, producing glycine and aldehydes
-
-
?
additional information
?
-
-
the enzyme also exhibits tetrahydrofolate-independent aldolase activity, EC 4.1.2.5, toward beta-hydroxyamino acids, producing glycine and aldehydes
-
-
?
additional information
?
-
-
no: D-serine
-
-
?
additional information
?
-
-
no: D-threonine
-
-
?
additional information
?
-
-
insoluble enzyme/antibody-complex shows 90% of original activity
-
-
?
additional information
?
-
the enzyme also catalyzes the tetrahydrofolate-independent retroaldol cleavage of L-allo-threonine and L-threonine to glycine and acetaldehyde
-
-
?
additional information
?
-
the enzyme also catalyzes the tetrahydrofolate-independent retroaldol cleavage of L-allo-threonine and L-threonine to glycine and acetaldehyde
-
-
?
additional information
?
-
SHM1 does not undergo half-transamination reaction with D-Ala resulting in the formation of the apoenzyme
-
-
?
additional information
?
-
SHM1 does not undergo half-transamination reaction with D-Ala resulting in the formation of the apoenzyme
-
-
?
additional information
?
-
-
SHM1 does not undergo half-transamination reaction with D-Ala resulting in the formation of the apoenzyme
-
-
?
additional information
?
-
SHM2 does not undergo half-transamination reaction with D-Ala resulting in the formation of the apoenzyme
-
-
?
additional information
?
-
SHM2 does not undergo half-transamination reaction with D-Ala resulting in the formation of the apoenzyme
-
-
?
additional information
?
-
-
SHM2 does not undergo half-transamination reaction with D-Ala resulting in the formation of the apoenzyme
-
-
?
additional information
?
-
SHM2 does not undergo half-transamination reaction with D-Ala resulting in the formation of the apoenzyme
-
-
?
additional information
?
-
SHM2 does not undergo half-transamination reaction with D-Ala resulting in the formation of the apoenzyme
-
-
?
additional information
?
-
SHM1 does not undergo half-transamination reaction with D-Ala resulting in the formation of the apoenzyme
-
-
?
additional information
?
-
SHM1 does not undergo half-transamination reaction with D-Ala resulting in the formation of the apoenzyme
-
-
?
additional information
?
-
-
no: L-threonine
-
-
?
additional information
?
-
-
review and comparison of enzyme activity, threonine aldolase and allothreonine aldolase activity from various sources
-
-
?
additional information
?
-
-
enzyme transaminates D-alanine to pyruvate and pyridoxamine phosphate
-
-
?
additional information
?
-
-
enzyme transaminates D-alanine to pyruvate and pyridoxamine phosphate
-
-
?
additional information
?
-
-
no: L-threonine
-
-
?
additional information
?
-
-
no: D-serine
-
-
?
additional information
?
-
-
review and comparison of enzyme activity, threonine aldolase and allothreonine aldolase activity from various sources
-
-
?
additional information
?
-
-
enzyme transaminates D-alanine to pyruvate and pyridoxamine phosphate
-
-
?
additional information
?
-
-
enzyme transaminates D-alanine to pyruvate and pyridoxamine phosphate
-
-
?
additional information
?
-
-
enzyme transaminates D-alanine to pyruvate and pyridoxamine phosphate
-
-
?
additional information
?
-
-
the enzyme also exhibits tetrahydrofolate-independent aldolase activity, EC 4.1.2.5, toward beta-hydroxyamino acids, producing glycine and aldehydes
-
-
?
additional information
?
-
-
no: L-threonine
-
-
?
additional information
?
-
-
no: D-serine
-
-
?
additional information
?
-
-
enzyme catalyzes the pyridoxal 5'-phosphate dependent reversible cleavage of 3-hydroxy-alpha-amino acids
-
-
?
additional information
?
-
-
enzyme catalyzes the pyridoxal 5'-phosphate dependent reversible cleavage of 3-hydroxy-alpha-amino acids
-
-
?
additional information
?
-
-
enzyme catalyzes the pyridoxal 5'-phosphate dependent reversible cleavage of 3-hydroxy-alpha-amino acids
-
-
?
additional information
?
-
-
mutant enzyme H230Y catalyses oxidation of NADH, not wild type enzyme, H230A, H230F, H230N
-
-
?
additional information
?
-
-
review and comparison of enzyme activity, threonine aldolase and allothreonine aldolase activity from various sources
-
-
?
additional information
?
-
-
enzyme transaminates D-alanine to pyruvate and pyridoxamine phosphate
-
-
?
additional information
?
-
-
enzyme transaminates D-alanine to pyruvate and pyridoxamine phosphate
-
-
?
additional information
?
-
-
enzyme transaminates D-alanine to pyruvate and pyridoxamine phosphate
-
-
?
additional information
?
-
-
enzyme transaminates D-alanine to pyruvate and pyridoxamine phosphate
-
-
?
additional information
?
-
-
enzyme catalyses the racemization of D- and L-alanine
-
-
?
additional information
?
-
-
the enzyme also exhibits THF-independent aldolase activity, EC 4.1.2.5, toward beta-hydroxyamino acids, producing glycine and aldehydes
-
-
?
additional information
?
-
-
-
-
-
?
additional information
?
-
-
review and comparison of enzyme activity, threonine aldolase and allothreonine aldolase activity from various sources
-
-
?
additional information
?
-
-
Plasmodium SHMT can use D-serine and L-serine as a substrate
-
-
?
additional information
?
-
-
SHMT also catalyzes the tetrahydrofolate-independent retro-aldol cleavage of 3-hydroxy amino acids
-
-
?
additional information
?
-
-
Plasmodium SHMT can use D-serine and L-serine as a substrate
-
-
?
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
-
-
?
additional information
?
-
the enzyme catalyzes the conversion of L- and D-serine to glycine in a THFdependent reaction
-
-
?
additional information
?
-
-
the enzyme catalyzes the conversion of L- and D-serine to glycine in a THFdependent reaction
-
-
?
additional information
?
-
L- and D-serine substrate binding structure analysis, overview
-
-
?
additional information
?
-
-
L- and D-serine substrate binding structure analysis, overview
-
-
?
additional information
?
-
SHMT catalyses the reversible cleavage of several beta-hydroxy amino acids varying in substituent and stereochemistry at Cbeta. The enzyme also has L-threo-beta-phenylserine aldolase activity
-
-
?
additional information
?
-
SHMT catalyses the reversible cleavage of several beta-hydroxy amino acids varying in substituent and stereochemistry at Cbeta. The enzyme also has L-threo-beta-phenylserine aldolase activity
-
-
?
additional information
?
-
-
no: L-threonine
-
-
?
additional information
?
-
-
no: L-threonine
-
-
?
additional information
?
-
-
no: D-serine
-
-
?
additional information
?
-
-
no: D-serine
-
-
?
additional information
?
-
-
enzyme catalyzes the pyridoxal 5'-phosphate dependent reversible cleavage of 3-hydroxy-alpha-amino acids
-
-
?
additional information
?
-
-
review and comparison of enzyme activity, threonine aldolase and allothreonine aldolase activity from various sources
-
-
?
additional information
?
-
-
enzyme transaminates D-alanine to pyruvate and pyridoxamine phosphate
-
-
?
additional information
?
-
-
enzyme transaminates D-alanine to pyruvate and pyridoxamine phosphate
-
-
?
additional information
?
-
-
no: D-allothreonine
-
-
?
additional information
?
-
-
no: D-allothreonine
-
-
?
additional information
?
-
-
no: D-threonine
-
-
?
additional information
?
-
-
low activity in placenta suggests that placental conversion of serine to glycine is not a major source of fetal glycine
-
-
?
additional information
?
-
-
no: L-threonine
-
-
?
additional information
?
-
-
no: D-serine
-
-
?
additional information
?
-
-
enzyme catalyzes the pyridoxal 5'-phosphate dependent reversible cleavage of 3-hydroxy-alpha-amino acids
-
-
?
additional information
?
-
-
enzyme transaminates D-alanine to pyruvate and pyridoxamine phosphate
-
-
?
additional information
?
-
-
no: D-allothreonine
-
-
?
additional information
?
-
-
-
-
-
?
additional information
?
-
-
-
-
-
?
additional information
?
-
-
no: L-threonine
-
-
?
additional information
?
-
-
enzyme transaminates D-alanine to pyruvate and pyridoxamine phosphate
-
-
?
additional information
?
-
the enzyme shows high serine hydroxymethyltransferase activity and L-serine production
-
-
?
additional information
?
-
-
the enzyme shows high serine hydroxymethyltransferase activity and L-serine production
-
-
?
additional information
?
-
-
review and comparison of enzyme activity, threonine aldolase and allothreonine aldolase activity from various sources
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
(6S)-tetrahydrofolate + D-serine
5,10-methylenetetrahydrofolate + glycine + H2O
(6S)-tetrahydrofolate + L-serine
5,10-methylenetetrahydrofolate + glycine + H2O
5,10-methylenetetrahydrofolate + glycine + H2O
tetrahydrofolate + D-serine
5,10-methylenetetrahydrofolate + glycine + H2O
tetrahydrofolate + L-Ser
-
the enzyme is a major source of one-carbon units for cellular metabolism. Potential for disruption of SHMT-mediated one-carbon metabolism by inadequate vitamin B-6 intake
-
-
r
5,10-methylenetetrahydrofolate + glycine + H2O
tetrahydrofolate + L-serine
L-Ser + tetrahydrofolate
Gly + 5,10-methylenetetrahydrofolate
-
placental conversion of serine to glycine is a major source of fetal glycine
-
-
?
L-serine + tetrahydrofolate
glycine + 5,10-methylenetetrahydrofolate + H2O
L-serine + tetrahydropteroylglutamate
glycine + 5,10-methylene-tetrahydropteroylglutamate + H2O
tetrahydrofolate + L-serine
5,10-methylenetetrahydrofolate + glycine + H2O
additional information
?
-
(6S)-tetrahydrofolate + D-serine
5,10-methylenetetrahydrofolate + glycine + H2O
-
-
-
-
r
(6S)-tetrahydrofolate + D-serine
5,10-methylenetetrahydrofolate + glycine + H2O
-
-
-
-
r
(6S)-tetrahydrofolate + L-serine
5,10-methylenetetrahydrofolate + glycine + H2O
-
-
-
r
(6S)-tetrahydrofolate + L-serine
5,10-methylenetetrahydrofolate + glycine + H2O
-
-
-
-
r
(6S)-tetrahydrofolate + L-serine
5,10-methylenetetrahydrofolate + glycine + H2O
-
-
-
-
r
5,10-methylenetetrahydrofolate + glycine + H2O
tetrahydrofolate + D-serine
-
-
-
-
r
5,10-methylenetetrahydrofolate + glycine + H2O
tetrahydrofolate + D-serine
-
-
-
-
r
5,10-methylenetetrahydrofolate + glycine + H2O
tetrahydrofolate + L-serine
-
-
-
-
r
5,10-methylenetetrahydrofolate + glycine + H2O
tetrahydrofolate + L-serine
-
-
-
-
r
5,10-methylenetetrahydrofolate + glycine + H2O
tetrahydrofolate + L-serine
-
-
-
-
r
5,10-methylenetetrahydrofolate + glycine + H2O
tetrahydrofolate + L-serine
-
-
-
-
r
5,10-methylenetetrahydrofolate + glycine + H2O
tetrahydrofolate + L-serine
-
-
-
r
5,10-methylenetetrahydrofolate + glycine + H2O
tetrahydrofolate + L-serine
-
-
-
r
5,10-methylenetetrahydrofolate + glycine + H2O
tetrahydrofolate + L-serine
-
-
-
-
r
5,10-methylenetetrahydrofolate + glycine + H2O
tetrahydrofolate + L-serine
-
-
-
-
r
5,10-methylenetetrahydrofolate + glycine + H2O
tetrahydrofolate + L-serine
-
-
-
-
r
5,10-methylenetetrahydrofolate + glycine + H2O
tetrahydrofolate + L-serine
-
-
-
-
r
5,10-methylenetetrahydrofolate + glycine + H2O
tetrahydrofolate + L-serine
-
-
-
r
5,10-methylenetetrahydrofolate + glycine + H2O
tetrahydrofolate + L-serine
-
-
-
r
5,10-methylenetetrahydrofolate + glycine + H2O
tetrahydrofolate + L-serine
-
-
-
r
5,10-methylenetetrahydrofolate + glycine + H2O
tetrahydrofolate + L-serine
-
-
-
r
5,10-methylenetetrahydrofolate + glycine + H2O
tetrahydrofolate + L-serine
-
-
-
r
5,10-methylenetetrahydrofolate + glycine + H2O
tetrahydrofolate + L-serine
-
-
-
r
5,10-methylenetetrahydrofolate + glycine + H2O
tetrahydrofolate + L-serine
-
-
-
-
?
5,10-methylenetetrahydrofolate + glycine + H2O
tetrahydrofolate + L-serine
-
-
-
r
5,10-methylenetetrahydrofolate + glycine + H2O
tetrahydrofolate + L-serine
-
-
-
r
5,10-methylenetetrahydrofolate + glycine + H2O
tetrahydrofolate + L-serine
-
-
-
-
r
5,10-methylenetetrahydrofolate + glycine + H2O
tetrahydrofolate + L-serine
-
-
-
r
5,10-methylenetetrahydrofolate + glycine + H2O
tetrahydrofolate + L-serine
-
-
-
r
5,10-methylenetetrahydrofolate + glycine + H2O
tetrahydrofolate + L-serine
-
-
-
-
r
5,10-methylenetetrahydrofolate + glycine + H2O
tetrahydrofolate + L-serine
-
-
-
r
5,10-methylenetetrahydrofolate + glycine + H2O
tetrahydrofolate + L-serine
-
-
-
r
5,10-methylenetetrahydrofolate + glycine + H2O
tetrahydrofolate + L-serine
-
-
-
r
5,10-methylenetetrahydrofolate + glycine + H2O
tetrahydrofolate + L-serine
-
-
-
r
5,10-methylenetetrahydrofolate + glycine + H2O
tetrahydrofolate + L-serine
-
-
-
r
5,10-methylenetetrahydrofolate + glycine + H2O
tetrahydrofolate + L-serine
-
-
-
r
5,10-methylenetetrahydrofolate + glycine + H2O
tetrahydrofolate + L-serine
-
-
-
-
r
5,10-methylenetetrahydrofolate + glycine + H2O
tetrahydrofolate + L-serine
-
-
-
-
r
5,10-methylenetetrahydrofolate + glycine + H2O
tetrahydrofolate + L-serine
-
-
-
-
?
5,10-methylenetetrahydrofolate + glycine + H2O
tetrahydrofolate + L-serine
-
-
-
-
?
5,10-methylenetetrahydrofolate + glycine + H2O
tetrahydrofolate + L-serine
-
-
-
-
r
5,10-methylenetetrahydrofolate + glycine + H2O
tetrahydrofolate + L-serine
-
-
-
r
5,10-methylenetetrahydrofolate + glycine + H2O
tetrahydrofolate + L-serine
-
-
-
r
5,10-methylenetetrahydrofolate + glycine + H2O
tetrahydrofolate + L-serine
-
-
-
r
5,10-methylenetetrahydrofolate + glycine + H2O
tetrahydrofolate + L-serine
-
-
-
r
5,10-methylenetetrahydrofolate + glycine + H2O
tetrahydrofolate + L-serine
-
-
-
r
5,10-methylenetetrahydrofolate + glycine + H2O
tetrahydrofolate + L-serine
-
-
-
-
?
5,10-methylenetetrahydrofolate + glycine + H2O
tetrahydrofolate + L-serine
-
-
-
-
r
5,10-methylenetetrahydrofolate + glycine + H2O
tetrahydrofolate + L-serine
-
-
-
-
?
5,10-methylenetetrahydrofolate + glycine + H2O
tetrahydrofolate + L-serine
-
-
-
-
r
5,10-methylenetetrahydrofolate + glycine + H2O
tetrahydrofolate + L-serine
-
-
-
-
r
5,10-methylenetetrahydrofolate + glycine + H2O
tetrahydrofolate + L-serine
-
-
-
-
r
5,10-methylenetetrahydrofolate + glycine + H2O
tetrahydrofolate + L-serine
-
-
-
-
?
5,10-methylenetetrahydrofolate + glycine + H2O
tetrahydrofolate + L-serine
-
-
-
-
r
5,10-methylenetetrahydrofolate + glycine + H2O
tetrahydrofolate + L-serine
-
-
-
-
r
5,10-methylenetetrahydrofolate + glycine + H2O
tetrahydrofolate + L-serine
-
-
-
r
5,10-methylenetetrahydrofolate + glycine + H2O
tetrahydrofolate + L-serine
-
-
-
r
5,10-methylenetetrahydrofolate + glycine + H2O
tetrahydrofolate + L-serine
-
-
-
r
5,10-methylenetetrahydrofolate + glycine + H2O
tetrahydrofolate + L-serine
-
-
-
r
5,10-methylenetetrahydrofolate + glycine + H2O
tetrahydrofolate + L-serine
-
-
-
r
5,10-methylenetetrahydrofolate + glycine + H2O
tetrahydrofolate + L-serine
-
-
-
-
r
5,10-methylenetetrahydrofolate + glycine + H2O
tetrahydrofolate + L-serine
-
-
-
r
5,10-methylenetetrahydrofolate + glycine + H2O
tetrahydrofolate + L-serine
-
-
-
r
5,10-methylenetetrahydrofolate + glycine + H2O
tetrahydrofolate + L-serine
-
-
-
r
5,10-methylenetetrahydrofolate + glycine + H2O
tetrahydrofolate + L-serine
-
-
-
-
r
5,10-methylenetetrahydrofolate + glycine + H2O
tetrahydrofolate + L-serine
-
-
-
-
r
5,10-methylenetetrahydrofolate + glycine + H2O
tetrahydrofolate + L-serine
-
-
-
r
5,10-methylenetetrahydrofolate + glycine + H2O
tetrahydrofolate + L-serine
-
-
-
r
5,10-methylenetetrahydrofolate + glycine + H2O
tetrahydrofolate + L-serine
-
-
-
r
5,10-methylenetetrahydrofolate + glycine + H2O
tetrahydrofolate + L-serine
-
-
-
r
5,10-methylenetetrahydrofolate + glycine + H2O
tetrahydrofolate + L-serine
-
-
-
r
5,10-methylenetetrahydrofolate + glycine + H2O
tetrahydrofolate + L-serine
-
-
-
r
5,10-methylenetetrahydrofolate + glycine + H2O
tetrahydrofolate + L-serine
-
-
-
r
L-serine + tetrahydrofolate
glycine + 5,10-methylenetetrahydrofolate + H2O
-
-
-
-
?
L-serine + tetrahydrofolate
glycine + 5,10-methylenetetrahydrofolate + H2O
-
may play important role in central nervous system
-
?
L-serine + tetrahydrofolate
glycine + 5,10-methylenetetrahydrofolate + H2O
-
-
-
?
L-serine + tetrahydrofolate
glycine + 5,10-methylenetetrahydrofolate + H2O
-
may play important role in central nervous system
-
?
L-serine + tetrahydrofolate
glycine + 5,10-methylenetetrahydrofolate + H2O
-
major pathway for production of C1-units of 5,10-methylenetetrahydrofolate
-
?
L-serine + tetrahydrofolate
glycine + 5,10-methylenetetrahydrofolate + H2O
-
major pathway for production of C1-units of 5,10-methylenetetrahydrofolate
-
?
L-serine + tetrahydrofolate
glycine + 5,10-methylenetetrahydrofolate + H2O
-
catalyzes interconversion of serine and glycine
-
?
L-serine + tetrahydrofolate
glycine + 5,10-methylenetetrahydrofolate + H2O
-
enzyme plays a pivotal role in channelling metabolites between amino acid and nucleotide metabolism
-
?
L-serine + tetrahydrofolate
glycine + 5,10-methylenetetrahydrofolate + H2O
-
-
-
?
L-serine + tetrahydrofolate
glycine + 5,10-methylenetetrahydrofolate + H2O
-
-
-
?
L-serine + tetrahydrofolate
glycine + 5,10-methylenetetrahydrofolate + H2O
-
main glycine source for purine biosynthetic pathway in ureide biogenesis
-
?
L-serine + tetrahydrofolate
glycine + 5,10-methylenetetrahydrofolate + H2O
-
main glycine source for purine biosynthetic pathway in ureide biogenesis
-
?
L-serine + tetrahydrofolate
glycine + 5,10-methylenetetrahydrofolate + H2O
-
-
-
-
?
L-serine + tetrahydrofolate
glycine + 5,10-methylenetetrahydrofolate + H2O
-
major pathway for production of C1-units of 5,10-methylenetetrahydrofolate
-
?
L-serine + tetrahydrofolate
glycine + 5,10-methylenetetrahydrofolate + H2O
-
major pathway for production of C1-units of 5,10-methylenetetrahydrofolate
-
?
L-serine + tetrahydrofolate
glycine + 5,10-methylenetetrahydrofolate + H2O
-
main glycine source for purine biosynthetic pathway in ureide biogenesis
-
?
L-serine + tetrahydrofolate
glycine + 5,10-methylenetetrahydrofolate + H2O
-
enzyme plays a pivotal role in channelling metabolites between amino acid and nucleotide metabolism
-
?
L-serine + tetrahydrofolate
glycine + 5,10-methylenetetrahydrofolate + H2O
-
key enzyme of serine pathway for assimilation of C1-compounds
-
?
L-serine + tetrahydrofolate
glycine + 5,10-methylenetetrahydrofolate + H2O
-
key enzyme of serine pathway for assimilation of C1-compounds
-
?
L-serine + tetrahydrofolate
glycine + 5,10-methylenetetrahydrofolate + H2O
-
regulatory protein
-
?
L-serine + tetrahydrofolate
glycine + 5,10-methylenetetrahydrofolate + H2O
-
main glycine source for purine biosynthetic pathway in ureide biogenesis
-
?
L-serine + tetrahydrofolate
glycine + 5,10-methylenetetrahydrofolate + H2O
-
key enzyme of serine pathway for assimilation of C1-compounds
-
?
L-serine + tetrahydrofolate
glycine + 5,10-methylenetetrahydrofolate + H2O
-
-
-
?
L-serine + tetrahydrofolate
glycine + 5,10-methylenetetrahydrofolate + H2O
-
may play important role in central nervous system
-
?
L-serine + tetrahydrofolate
glycine + 5,10-methylenetetrahydrofolate + H2O
-
-
-
?
L-serine + tetrahydrofolate
glycine + 5,10-methylenetetrahydrofolate + H2O
-
-
-
?
L-serine + tetrahydrofolate
glycine + 5,10-methylenetetrahydrofolate + H2O
-
enzyme is a component of thymidylate cycle
-
?
L-serine + tetrahydrofolate
glycine + 5,10-methylenetetrahydrofolate + H2O
-
may play important role in central nervous system
-
?
L-serine + tetrahydrofolate
glycine + 5,10-methylenetetrahydrofolate + H2O
-
catalyzes interconversion of serine and glycine
-
?
L-serine + tetrahydrofolate
glycine + 5,10-methylenetetrahydrofolate + H2O
-
enzyme plays a pivotal role in channelling metabolites between amino acid and nucleotide metabolism
-
?
L-serine + tetrahydrofolate
glycine + 5,10-methylenetetrahydrofolate + H2O
-
-
-
?
L-serine + tetrahydrofolate
glycine + 5,10-methylenetetrahydrofolate + H2O
-
-
-
?
L-serine + tetrahydrofolate
glycine + 5,10-methylenetetrahydrofolate + H2O
-
enzyme is a component of thymidylate cycle
-
?
L-serine + tetrahydrofolate
glycine + 5,10-methylenetetrahydrofolate + H2O
-
may play important role in central nervous system
-
?
L-serine + tetrahydrofolate
glycine + 5,10-methylenetetrahydrofolate + H2O
-
enzyme plays a pivotal role in channelling metabolites between amino acid and nucleotide metabolism
-
?
L-serine + tetrahydrofolate
glycine + 5,10-methylenetetrahydrofolate + H2O
-
-
-
?
L-serine + tetrahydrofolate
glycine + 5,10-methylenetetrahydrofolate + H2O
-
enzyme plays a pivotal role in channelling metabolites between amino acid and nucleotide metabolism
-
?
L-serine + tetrahydrofolate
glycine + 5,10-methylenetetrahydrofolate + H2O
-
major pathway for production of C1-units of 5,10-methylenetetrahydrofolate
-
?
L-serine + tetrahydrofolate
glycine + 5,10-methylenetetrahydrofolate + H2O
-
major pathway for production of C1-units of 5,10-methylenetetrahydrofolate
-
?
L-serine + tetrahydrofolate
glycine + 5,10-methylenetetrahydrofolate + H2O
-
catalyzes interconversion of serine and glycine
-
?
L-serine + tetrahydrofolate
glycine + 5,10-methylenetetrahydrofolate + H2O
key enzyme of serine pathway for assimilation of C1-compounds
-
?
L-serine + tetrahydrofolate
glycine + 5,10-methylenetetrahydrofolate + H2O
key enzyme of serine pathway for assimilation of C1-compounds
-
?
L-serine + tetrahydrofolate
glycine + 5,10-methylenetetrahydrofolate + H2O
-
-
-
?
L-serine + tetrahydrofolate
glycine + 5,10-methylenetetrahydrofolate + H2O
-
key enzyme of serine pathway for assimilation of C1-compounds
-
?
L-serine + tetrahydrofolate
glycine + 5,10-methylenetetrahydrofolate + H2O
-
enzyme plays a pivotal role in channelling metabolites between amino acid and nucleotide metabolism
-
?
L-serine + tetrahydrofolate
glycine + 5,10-methylenetetrahydrofolate + H2O
-
key enzyme of serine pathway for assimilation of C1-compounds
-
?
L-serine + tetrahydrofolate
glycine + 5,10-methylenetetrahydrofolate + H2O
-
may play important role in central nervous system
-
?
L-serine + tetrahydrofolate
glycine + 5,10-methylenetetrahydrofolate + H2O
-
-
-
?
L-serine + tetrahydrofolate
glycine + 5,10-methylenetetrahydrofolate + H2O
-
regulatory protein
-
?
L-serine + tetrahydrofolate
glycine + 5,10-methylenetetrahydrofolate + H2O
-
key enzyme of serine pathway for assimilation of C1-compounds
-
?
L-serine + tetrahydropteroylglutamate
glycine + 5,10-methylene-tetrahydropteroylglutamate + H2O
-
-
-
-
r
L-serine + tetrahydropteroylglutamate
glycine + 5,10-methylene-tetrahydropteroylglutamate + H2O
-
-
-
-
r
tetrahydrofolate + L-serine
5,10-methylenetetrahydrofolate + glycine + H2O
-
-
-
-
r
tetrahydrofolate + L-serine
5,10-methylenetetrahydrofolate + glycine + H2O
-
-
-
-
r
tetrahydrofolate + L-serine
5,10-methylenetetrahydrofolate + glycine + H2O
-
-
-
-
r
tetrahydrofolate + L-serine
5,10-methylenetetrahydrofolate + glycine + H2O
-
-
-
-
r
tetrahydrofolate + L-serine
5,10-methylenetetrahydrofolate + glycine + H2O
-
-
-
-
r
tetrahydrofolate + L-serine
5,10-methylenetetrahydrofolate + glycine + H2O
-
-
-
-
r
tetrahydrofolate + L-serine
5,10-methylenetetrahydrofolate + glycine + H2O
-
-
-
-
r
tetrahydrofolate + L-serine
5,10-methylenetetrahydrofolate + glycine + H2O
-
-
-
r
tetrahydrofolate + L-serine
5,10-methylenetetrahydrofolate + glycine + H2O
-
-
-
r
tetrahydrofolate + L-serine
5,10-methylenetetrahydrofolate + glycine + H2O
-
-
-
r
tetrahydrofolate + L-serine
5,10-methylenetetrahydrofolate + glycine + H2O
-
-
-
-
r
tetrahydrofolate + L-serine
5,10-methylenetetrahydrofolate + glycine + H2O
-
-
-
r
tetrahydrofolate + L-serine
5,10-methylenetetrahydrofolate + glycine + H2O
-
-
-
r
tetrahydrofolate + L-serine
5,10-methylenetetrahydrofolate + glycine + H2O
-
-
-
-
r
tetrahydrofolate + L-serine
5,10-methylenetetrahydrofolate + glycine + H2O
-
-
-
r
tetrahydrofolate + L-serine
5,10-methylenetetrahydrofolate + glycine + H2O
-
-
-
r
tetrahydrofolate + L-serine
5,10-methylenetetrahydrofolate + glycine + H2O
-
-
-
r
tetrahydrofolate + L-serine
5,10-methylenetetrahydrofolate + glycine + H2O
-
-
-
r
tetrahydrofolate + L-serine
5,10-methylenetetrahydrofolate + glycine + H2O
-
-
-
r
tetrahydrofolate + L-serine
5,10-methylenetetrahydrofolate + glycine + H2O
-
-
-
-
r
tetrahydrofolate + L-serine
5,10-methylenetetrahydrofolate + glycine + H2O
-
-
-
r
tetrahydrofolate + L-serine
5,10-methylenetetrahydrofolate + glycine + H2O
-
-
-
r
tetrahydrofolate + L-serine
5,10-methylenetetrahydrofolate + glycine + H2O
-
-
-
r
tetrahydrofolate + L-serine
5,10-methylenetetrahydrofolate + glycine + H2O
-
-
-
-
r
tetrahydrofolate + L-serine
5,10-methylenetetrahydrofolate + glycine + H2O
-
-
-
-
r
tetrahydrofolate + L-serine
5,10-methylenetetrahydrofolate + glycine + H2O
-
-
-
-
r
tetrahydrofolate + L-serine
5,10-methylenetetrahydrofolate + glycine + H2O
-
-
-
-
r
tetrahydrofolate + L-serine
5,10-methylenetetrahydrofolate + glycine + H2O
-
-
-
r
tetrahydrofolate + L-serine
5,10-methylenetetrahydrofolate + glycine + H2O
-
-
-
r
tetrahydrofolate + L-serine
5,10-methylenetetrahydrofolate + glycine + H2O
-
-
-
r
tetrahydrofolate + L-serine
5,10-methylenetetrahydrofolate + glycine + H2O
-
-
-
r
tetrahydrofolate + L-serine
5,10-methylenetetrahydrofolate + glycine + H2O
-
-
-
r
tetrahydrofolate + L-serine
5,10-methylenetetrahydrofolate + glycine + H2O
-
-
-
r
tetrahydrofolate + L-serine
5,10-methylenetetrahydrofolate + glycine + H2O
-
-
-
-
r
tetrahydrofolate + L-serine
5,10-methylenetetrahydrofolate + glycine + H2O
-
-
-
-
r
tetrahydrofolate + L-serine
5,10-methylenetetrahydrofolate + glycine + H2O
-
-
-
r
tetrahydrofolate + L-serine
5,10-methylenetetrahydrofolate + glycine + H2O
-
-
-
r
tetrahydrofolate + L-serine
5,10-methylenetetrahydrofolate + glycine + H2O
-
-
-
r
additional information
?
-
-
SHMT1 functions in the photorespiratory pathway and plays a critical role in controlling the cell damage provoked by abiotic stresses such as high light and salt and in restricting pathogen induced cell death
-
-
?
additional information
?
-
-
SHMT1 functions in the photorespiratory pathway and plays a critical role in controlling the cell damage provoked by abiotic stresses such as high light and salt and in restricting pathogen induced cell death
-
-
?
additional information
?
-
-
SHMT also catalyzes the hydrolysis of 5,10-methenyl-tetrahydropteroylglutamate to 5-formyl-tetrahydropteroylglutamate
-
-
?
additional information
?
-
disruption of the SHM2 gene, encoding one of two serine hydroxymethyltransferase isoenzymes, reduces the flux from glycine to serine
-
-
?
additional information
?
-
-
disruption of the SHM2 gene, encoding one of two serine hydroxymethyltransferase isoenzymes, reduces the flux from glycine to serine
-
-
?
additional information
?
-
-
SHMT also catalyzes the hydrolysis of 5,10-methenyl-tetrahydropteroylglutamate to 5-formyl-tetrahydropteroylglutamate
-
-
?
additional information
?
-
-
low activity in placenta suggests that placental conversion of serine to glycine is not a major source of fetal glycine
-
-
?
additional information
?
-
-
the enzyme plays an indispensable role in nucleic acid biosynthesis
-
-
?
additional information
?
-
-
Plasmodium SHMT can use D-serine and L-serine as a substrate
-
-
?
additional information
?
-
-
Plasmodium SHMT can use D-serine and L-serine as a substrate
-
-
?
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
-
-
?
additional information
?
-
the enzyme catalyzes the conversion of L- and D-serine to glycine in a THFdependent reaction
-
-
?
additional information
?
-
-
the enzyme catalyzes the conversion of L- and D-serine to glycine in a THFdependent reaction
-
-
?
additional information
?
-
SHMT catalyses the reversible cleavage of several beta-hydroxy amino acids varying in substituent and stereochemistry at Cbeta. The enzyme also has L-threo-beta-phenylserine aldolase activity
-
-
?
additional information
?
-
SHMT catalyses the reversible cleavage of several beta-hydroxy amino acids varying in substituent and stereochemistry at Cbeta. The enzyme also has L-threo-beta-phenylserine aldolase activity
-
-
?
additional information
?
-
-
low activity in placenta suggests that placental conversion of serine to glycine is not a major source of fetal glycine
-
-
?
additional information
?
-
the enzyme shows high serine hydroxymethyltransferase activity and L-serine production
-
-
?
additional information
?
-
-
the enzyme shows high serine hydroxymethyltransferase activity and L-serine production
-
-
?
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(+/-)-methyl 5-[3-(6-amino-5-cyano-4-isopropyl-3-methyl-1,4-dihydropyrano[2,3-c]pyrazol-4-yl)-5-cyanophenyl]thiophene-2-carboxylate
-
-
(4R)-6-amino-4-(5-cyano-3'-fluoro[1,1'-biphenyl]-3-yl)-3-methyl-4-(propan-2-yl)-2,4-dihydropyrano[2,3-c]pyrazole-5-carbonitrile
(4R,4S)-5-cyano-4-(3-cyano-5-[5-[((S)-1,3-dicarboxypropyl)-carbamoyl]thiophen-2-yl]phenyl)-3-methyl-4-(propan-2-yl)-2,4-dihydropyrano[2,3-c]pyrazol-6-aminium trifluoroacetate
(4S)-6-amino-4-(5-cyano-3'-fluoro[1,1'-biphenyl]-3-yl)-3-methyl-4-(propan-2-yl)-2,4-dihydropyrano[2,3-c]pyrazole-5-carbonitrile
2-mercaptopropionic acid
-
-
3'-[6-amino-5-cyano-3-methyl-4-(propan-2-yl)-2,4-dihydropyrano[2,3-c]pyrazol-4-yl]-5'-cyano[1,1'-biphenyl]-3-carboxylic acid
3-Bromopyruvate
isoform SHMT1 is completely inhibited by 3-bromopyruvate; isoform SHMT2 retains a significant fraction of activity with 3-bromopyruvate
5,10-methenyltetrahydrofolate
-
-
5,10-methylene-5,6,7,8-tetrahydrofolic acid
-
-
5,5-dithiobis(2-nitrobenzoic acid)
5-formyltetrahydrofolate
-
can inhibit SHMT in vivo and thereby influence glycine pool size, can accumulate glycine in both wild-type and 5-CHO-THF cycloligase mutant
5-formyltetrahydrofolate monoglutamate
5-methyl-5,6,7,8-tetrahydrofolate
-
-
5-methyltetrahydrofolate monoglutamate
5-Methyltetrahydrofolate triglutamate
5-[3-[6-amino-5-cyano-3-methyl-4-(propan-2-yl)-2,4-dihydropyrano[2,3-c]pyrazol-4-yl]-5-cyanophenyl]-N,N-dimethylthiophene-2-carboxamide
5-[3-[6-amino-5-cyano-3-methyl-4-(propan-2-yl)-2,4-dihydropyrano[2,3-c]pyrazol-4-yl]-5-cyanophenyl]-N-[3-(diethylamino)propyl]thiophene-2-carboxamide
5-[3-[6-amino-5-cyano-3-methyl-4-(propan-2-yl)-2,4-dihydropyrano[2,3-c]pyrazol-4-yl]-5-cyanophenyl]thiophene-2-carboxylic acid
6-amino-3-methyl-4-[3-(morpholin-4-yl)-5-(trifluoromethyl)phenyl]-4-(propan-2-yl)-2,4-dihydropyrano[2,3-c]pyrazole-5-carbonitrile
6-amino-4-(3,5-dichlorophenyl)-3-methyl-4-(propan-2-yl)-2,4-dihydropyrano[2,3-c]pyrazole-5-carbonitrile
6-amino-4-(5-cyano-3'-fluoro[1,1'-biphenyl]-3-yl)-3-methyl-4-(propan-2-yl)-2,4-dihydropyrano[2,3-c]pyrazole-5-carbonitrile
6-amino-4-[3-cyano-5-(piperazin-1-yl)phenyl]-3-methyl-4-(propan-2-yl)-2,4-dihydropyrano[2,3-c]pyrazole-5-carbonitril
-
-
6-amino-4-[3-cyano-5-(piperazin-1-yl)phenyl]-3-methyl-4-(propan-2-yl)-2,4-dihydropyrano[2,3-c]pyrazole-5-carbonitrile
-
6-amino-5-cyano-4-[3-cyano-5-(5-[[3-(morpholin-4-ium-4-yl)propyl]carbamoyl]thiophen-2-yl)phenyl]-3-methyl-4-isopropyl-2,4-dihydropyrano[2,3-c]pyrazol-1-ium bis-(trifluoroacetate)
Antibodies to cytosolic enzyme
-
-
-
Antibodies to mitochondrial enzyme
-
no inhibition of cytosolic enzyme
-
benzyl 4-[3-[6-amino-5-cyano-3-methyl-4-(propan-2-yl)-2,4-dihydropyrano[2,3-c]pyrazol-4-yl]-5-cyanophenyl]piperazine-1-carboxylate
benzyl 5-[3-[(4R)-6-amino-5-cyano-3-methyl-4-(propan-2-yl)-2,4-dihydropyrano[2,3-c]pyrazol-4-yl]-5-cyanophenyl]thiophene-2-carboxylate
benzyl 5-[3-[(4S)-6-amino-5-cyano-3-methyl-4-(propan-2-yl)-2,4-dihydropyrano[2,3-c]pyrazol-4-yl]-5-cyanophenyl]thiophene-2-carboxylate
benzyl 5-[3-[6-amino-5-cyano-3-methyl-4-(propan-2-yl)-2,4-dihydropyrano[2,3-c]pyrazol-4-yl]-5-cyanophenyl]thiophene-2-carboxylate
beta-chloroalanine
-
suicide substrate
beta-trifluoroallothreonine
carboxymethoxylamine
-
strong
CO(NH2)2
60.59% residual activity at 1 mM
dithiothreitol
59.29% residual activity at 1 mM
ethyl 4-[[3-[6-amino-5-cyano-3-methyl-4-(propan-2-yl)-2,4-dihydropyrano[2,3-c]pyrazol-4-yl]-5-cyanophenyl](methyl)amino]butanoate
guanidine hydrochloride
86% loss of activity at 0.25 M
L-alpha,beta-diaminopropionic acid
-
-
L-mimosine
-
inhibits SHMT1 transcription by chelating zinc, eliminates the metal regulatory element- and Sp1-binding activity in nuclear extracts from MCF-7 cells, but not in nuclear extracts from the mimosine-resistant cell line, MCF-7/2a
leucovorin
leucovorin (N5-CHO-THF) exhibits a differential inhibition pattern: it significantly inhibits the aldol cleavage of serine catalyzed by zebrafish cytosolic SHMT but it inhibits to a lesser extent the reaction catalyzed by the mitochondrial isozyme. Approximately 70% and 30% inhibition are observed for zebrafish cytosolic- and zebrafish mitochondrial SHMT activities, respectively, in the presence of 70 mM leucovorin. An even larger difference between both isoenzymes is observed when the inhibition is assayed in the presence of 50 mM serine; leucovorin (N5-CHO-THF) exhibits a differential inhibition pattern: it significantly inhibits the aldol cleavage of serine catalyzed by zebrafish cytosolic SHMT but it inhibits to a lesser extent the reaction catalyzed by the mitochondrial isozyme. Approximately 70% and 30% inhibition are observed for zebrafish cytosolic- and zebrafish mitochondrial SHMT activities, respectively, in the presence of 70 mM leucovorin. An even larger difference between both isoenzymes is observed when the inhibition is assayed in the presence of 50 mM serine
methyl 3'-[6-amino-5-cyano-3-methyl-4-(propan-2-yl)-2,4-dihydropyrano[2,3-c]pyrazol-4-yl]-5'-chloro[1,1'-biphenyl]-4-carboxylate
methyl 5-[3-[(4R)-6-amino-5-cyano-3-methyl-4-(propan-2-yl)-2,4-dihydropyrano[2,3-c]pyrazol-4-yl]-5-cyanophenyl]thiophene-2-carboxylate
methyl 5-[3-[(4S)-6-amino-5-cyano-3-methyl-4-(propan-2-yl)-2,4-dihydropyrano[2,3-c]pyrazol-4-yl]-5-cyanophenyl]thiophene-2-carboxylate
methyl 5-[3-[6-amino-5-cyano-3-methyl-4-(propan-2-yl)-2,4-dihydropyrano[2,3-c]pyrazol-4-yl]-5-cyanophenyl]thiophene-2-carboxylate
-
-
methyl methanethiosulfonate
nolatrexed
-
poor inhibition
phenylhydrazine
-
partially reversible by pyridoxal 5'-phosphate
S-adenosyl-L-methionine
-
-
substituted hydroxylamine derivates
-
sulfonyl fluoride triazine derivates
tetrahydrofolate derivatives
-
tetrahydropteroylglutamate
-
(4R)-6-amino-4-(5-cyano-3'-fluoro[1,1'-biphenyl]-3-yl)-3-methyl-4-(propan-2-yl)-2,4-dihydropyrano[2,3-c]pyrazole-5-carbonitrile
-
-
(4R)-6-amino-4-(5-cyano-3'-fluoro[1,1'-biphenyl]-3-yl)-3-methyl-4-(propan-2-yl)-2,4-dihydropyrano[2,3-c]pyrazole-5-carbonitrile
-
(4R,4S)-5-cyano-4-(3-cyano-5-[5-[((S)-1,3-dicarboxypropyl)-carbamoyl]thiophen-2-yl]phenyl)-3-methyl-4-(propan-2-yl)-2,4-dihydropyrano[2,3-c]pyrazol-6-aminium trifluoroacetate
-
-
(4R,4S)-5-cyano-4-(3-cyano-5-[5-[((S)-1,3-dicarboxypropyl)-carbamoyl]thiophen-2-yl]phenyl)-3-methyl-4-(propan-2-yl)-2,4-dihydropyrano[2,3-c]pyrazol-6-aminium trifluoroacetate
-
(4S)-6-amino-4-(5-cyano-3'-fluoro[1,1'-biphenyl]-3-yl)-3-methyl-4-(propan-2-yl)-2,4-dihydropyrano[2,3-c]pyrazole-5-carbonitrile
-
-
(4S)-6-amino-4-(5-cyano-3'-fluoro[1,1'-biphenyl]-3-yl)-3-methyl-4-(propan-2-yl)-2,4-dihydropyrano[2,3-c]pyrazole-5-carbonitrile
-
1,10-phenanthroline
-
-
3'-[6-amino-5-cyano-3-methyl-4-(propan-2-yl)-2,4-dihydropyrano[2,3-c]pyrazol-4-yl]-5'-cyano[1,1'-biphenyl]-3-carboxylic acid
-
-
3'-[6-amino-5-cyano-3-methyl-4-(propan-2-yl)-2,4-dihydropyrano[2,3-c]pyrazol-4-yl]-5'-cyano[1,1'-biphenyl]-3-carboxylic acid
-
4-chloro-L-threonine
-
-
5,5-dithiobis(2-nitrobenzoic acid)
-
-
5,5-dithiobis(2-nitrobenzoic acid)
-
-
5-formyltetrahydrofolate monoglutamate
-
-
5-formyltetrahydrofolate monoglutamate
-
-
5-methyltetrahydrofolate monoglutamate
-
-
5-methyltetrahydrofolate monoglutamate
-
-
5-Methyltetrahydrofolate triglutamate
-
-
5-Methyltetrahydrofolate triglutamate
-
-
5-[3-[6-amino-5-cyano-3-methyl-4-(propan-2-yl)-2,4-dihydropyrano[2,3-c]pyrazol-4-yl]-5-cyanophenyl]-N,N-dimethylthiophene-2-carboxamide
-
-
5-[3-[6-amino-5-cyano-3-methyl-4-(propan-2-yl)-2,4-dihydropyrano[2,3-c]pyrazol-4-yl]-5-cyanophenyl]-N,N-dimethylthiophene-2-carboxamide
-
5-[3-[6-amino-5-cyano-3-methyl-4-(propan-2-yl)-2,4-dihydropyrano[2,3-c]pyrazol-4-yl]-5-cyanophenyl]-N-[3-(diethylamino)propyl]thiophene-2-carboxamide
-
-
5-[3-[6-amino-5-cyano-3-methyl-4-(propan-2-yl)-2,4-dihydropyrano[2,3-c]pyrazol-4-yl]-5-cyanophenyl]-N-[3-(diethylamino)propyl]thiophene-2-carboxamide
-
5-[3-[6-amino-5-cyano-3-methyl-4-(propan-2-yl)-2,4-dihydropyrano[2,3-c]pyrazol-4-yl]-5-cyanophenyl]thiophene-2-carboxylic acid
-
-
5-[3-[6-amino-5-cyano-3-methyl-4-(propan-2-yl)-2,4-dihydropyrano[2,3-c]pyrazol-4-yl]-5-cyanophenyl]thiophene-2-carboxylic acid
-
6-amino-3-methyl-4-[3-(morpholin-4-yl)-5-(trifluoromethyl)phenyl]-4-(propan-2-yl)-2,4-dihydropyrano[2,3-c]pyrazole-5-carbonitrile
-
-
6-amino-3-methyl-4-[3-(morpholin-4-yl)-5-(trifluoromethyl)phenyl]-4-(propan-2-yl)-2,4-dihydropyrano[2,3-c]pyrazole-5-carbonitrile
-
6-amino-4-(3,5-dichlorophenyl)-3-methyl-4-(propan-2-yl)-2,4-dihydropyrano[2,3-c]pyrazole-5-carbonitrile
-
-
6-amino-4-(3,5-dichlorophenyl)-3-methyl-4-(propan-2-yl)-2,4-dihydropyrano[2,3-c]pyrazole-5-carbonitrile
-
6-amino-4-(5-cyano-3'-fluoro[1,1'-biphenyl]-3-yl)-3-methyl-4-(propan-2-yl)-2,4-dihydropyrano[2,3-c]pyrazole-5-carbonitrile
-
-
6-amino-4-(5-cyano-3'-fluoro[1,1'-biphenyl]-3-yl)-3-methyl-4-(propan-2-yl)-2,4-dihydropyrano[2,3-c]pyrazole-5-carbonitrile
-
6-amino-5-cyano-4-[3-cyano-5-(5-[[3-(morpholin-4-ium-4-yl)propyl]carbamoyl]thiophen-2-yl)phenyl]-3-methyl-4-isopropyl-2,4-dihydropyrano[2,3-c]pyrazol-1-ium bis-(trifluoroacetate)
-
-
6-amino-5-cyano-4-[3-cyano-5-(5-[[3-(morpholin-4-ium-4-yl)propyl]carbamoyl]thiophen-2-yl)phenyl]-3-methyl-4-isopropyl-2,4-dihydropyrano[2,3-c]pyrazol-1-ium bis-(trifluoroacetate)
-
aminopterin
-
-
benzyl 4-[3-[6-amino-5-cyano-3-methyl-4-(propan-2-yl)-2,4-dihydropyrano[2,3-c]pyrazol-4-yl]-5-cyanophenyl]piperazine-1-carboxylate
-
-
benzyl 4-[3-[6-amino-5-cyano-3-methyl-4-(propan-2-yl)-2,4-dihydropyrano[2,3-c]pyrazol-4-yl]-5-cyanophenyl]piperazine-1-carboxylate
-
benzyl 5-[3-[(4R)-6-amino-5-cyano-3-methyl-4-(propan-2-yl)-2,4-dihydropyrano[2,3-c]pyrazol-4-yl]-5-cyanophenyl]thiophene-2-carboxylate
-
-
benzyl 5-[3-[(4R)-6-amino-5-cyano-3-methyl-4-(propan-2-yl)-2,4-dihydropyrano[2,3-c]pyrazol-4-yl]-5-cyanophenyl]thiophene-2-carboxylate
-
benzyl 5-[3-[(4S)-6-amino-5-cyano-3-methyl-4-(propan-2-yl)-2,4-dihydropyrano[2,3-c]pyrazol-4-yl]-5-cyanophenyl]thiophene-2-carboxylate
-
-
benzyl 5-[3-[(4S)-6-amino-5-cyano-3-methyl-4-(propan-2-yl)-2,4-dihydropyrano[2,3-c]pyrazol-4-yl]-5-cyanophenyl]thiophene-2-carboxylate
-
benzyl 5-[3-[6-amino-5-cyano-3-methyl-4-(propan-2-yl)-2,4-dihydropyrano[2,3-c]pyrazol-4-yl]-5-cyanophenyl]thiophene-2-carboxylate
-
-
benzyl 5-[3-[6-amino-5-cyano-3-methyl-4-(propan-2-yl)-2,4-dihydropyrano[2,3-c]pyrazol-4-yl]-5-cyanophenyl]thiophene-2-carboxylate
-
beta-Alanine
-
-
beta-trifluoroallothreonine
-
-
beta-trifluoroallothreonine
-
-
beta-trifluoroallothreonine
-
-
beta-trifluoroallothreonine
-
-
beta-trifluoroallothreonine
-
-
beta-trifluorothreonine
-
-
beta-trifluorothreonine
-
-
beta-trifluorothreonine
-
-
beta-trifluorothreonine
-
-
beta-trifluorothreonine
-
-
beta-trifluorothreonine
-
-
Bromopyruvate
-
irreversible inactivation, substrates partially protect
Bromopyruvate
-
only cytoplasmac not mitochondrial enzyme
Chloroacetaldehyde
-
irreversible inactivation, substrates partially protect
Chloroacetaldehyde
-
only cytoplasmic not mitochondrial enzyme
Cibacron blue F3GA
-
reversible by dialysis
Cibacron blue F3GA
-
complete inhibition, NAD(H) protects, reversible by tetrahydrofolate
Co2+
-
strong inhibition at 1 mM
Co2+
60.03% residual activity at 1 mM
Co2+
strong inhibition at 1 mM
Co2+
slight inhibition; strong inhibition
CTAB
-
-
Cu2+
-
strong inhibition
Cu2+
-
strong inhibition at 1 mM
Cu2+
8.95% residual activity at 1 mM
Cu2+
strong inhibition at 1 mM
D-alanine
-
-
D-alanine
-
inactivates enzyme by converting the enzyme bound pyridoxal 5'-phosphate to pyridoxamine phosphate in a transamination reaction
D-alanine
inactivates enzyme by converting the enzyme bound pyridoxal 5'-phosphate to pyridoxamine phosphate in a transamination reaction
D-alanine
-
inactivates enzyme by converting the enzyme bound pyridoxal 5'-phosphate to pyridoxamine phosphate in a transamination reaction
D-beta-fluoroalanine
-
-
D-cycloserine
-
-
D-cycloserine
-
overexpression of SHMT-S increases resistance in a rich folate containing medium
D-cycloserine
-
interaction extreme rapidly and irreversible
Dichloromethotrexate
-
-
DL-2-methylserine
-
-
ethyl 4-[[3-[6-amino-5-cyano-3-methyl-4-(propan-2-yl)-2,4-dihydropyrano[2,3-c]pyrazol-4-yl]-5-cyanophenyl](methyl)amino]butanoate
-
-
ethyl 4-[[3-[6-amino-5-cyano-3-methyl-4-(propan-2-yl)-2,4-dihydropyrano[2,3-c]pyrazol-4-yl]-5-cyanophenyl](methyl)amino]butanoate
-
Fe2+
-
strong inhibition at 1 mM
Fe2+
complete inhibition at 1 mM
Fe2+
strong inhibition at 1 mM
formaldehyde
inactivation
formaldehyde
inactivation
Glycidaldehyde
-
directed to C1-binding-site
Glycidaldehyde
-
only cytoplasmic enzyme
glycine
-
-
glycine
-
glycine inhibits His6-tagged SHMT competitively with respect to serine and non-competitively with respect to tetrahydrofolate
Hg2+
-
strong inhibition at 1 mM
Hg2+
complete inhibition at 1 mM
Hg2+
strong inhibition at 1 mM
iodoacetamide
-
irreversible inactivation, substrates partially protect
iodoacetamide
-
only cytoplasmic not mitochondrial enzyme
KCl
-
-
L-alanine
-
-
L-amino acids
-
-
L-amino acids
-
weak, e.g. L-aspartic acid, ornithine, lysine, methionine, phenylalanine, homoserine, threonine, 4-aminobutyric acid
L-cysteine
-
-
L-cysteine
-
mitochondrial enzyme
L-methionine
-
not
L-serine
-
-
L-serine
-
competitive to glycine
lometrexol
-
competitive inhibition
lometrexol
49.7% residual activity at 0.1 mM
methotrexate
-
-
methotrexate
87.4% residual activity at 0.1 mM
methyl 3'-[6-amino-5-cyano-3-methyl-4-(propan-2-yl)-2,4-dihydropyrano[2,3-c]pyrazol-4-yl]-5'-chloro[1,1'-biphenyl]-4-carboxylate
-
-
methyl 3'-[6-amino-5-cyano-3-methyl-4-(propan-2-yl)-2,4-dihydropyrano[2,3-c]pyrazol-4-yl]-5'-chloro[1,1'-biphenyl]-4-carboxylate
-
methyl 5-[3-[(4R)-6-amino-5-cyano-3-methyl-4-(propan-2-yl)-2,4-dihydropyrano[2,3-c]pyrazol-4-yl]-5-cyanophenyl]thiophene-2-carboxylate
-
-
methyl 5-[3-[(4R)-6-amino-5-cyano-3-methyl-4-(propan-2-yl)-2,4-dihydropyrano[2,3-c]pyrazol-4-yl]-5-cyanophenyl]thiophene-2-carboxylate
-
methyl 5-[3-[(4S)-6-amino-5-cyano-3-methyl-4-(propan-2-yl)-2,4-dihydropyrano[2,3-c]pyrazol-4-yl]-5-cyanophenyl]thiophene-2-carboxylate
-
-
methyl 5-[3-[(4S)-6-amino-5-cyano-3-methyl-4-(propan-2-yl)-2,4-dihydropyrano[2,3-c]pyrazol-4-yl]-5-cyanophenyl]thiophene-2-carboxylate
-
methyl methanethiosulfonate
-
-
methyl methanethiosulfonate
-
-
methyl methanethiosulfonate
-
-
methyl methanethiosulfonate
-
-
methyl methanethiosulfonate
-
-
Mn2+
-
strong inhibition at 1 mM
Mn2+
60.81% residual activity at 1 mM
Mn2+
strong inhibition at 1 mM
NaCl
60% inhibition at 100 mM, restored to 66-71% activity in presence of 50 mM glycine betaine
NH2OH
-
-
PCMB
-
strong
pemetrexed
-
i.e. (S)-2-[4-[2-(4-amino-2-oxo-3,5,7-triazabicyclo[4.3.0]nona-3,8,10-trien-9-yl) ethyl] benzoyl]aminopentanedioic acid, brand name Alimta, low micromolar inhibitor
pemetrexed
79.2% residual activity at 0.1 mM
raltitrexed
-
-
raltitrexed
94% residual activity at 0.1 mM
SDS
-
strong inhibition
substituted hydroxylamine derivates
-
-
-
substituted hydroxylamine derivates
-
-
-
substituted hydroxylamine derivates
-
-
-
substituted hydroxylamine derivates
-
-
-
substituted hydroxylamine derivates
-
-
-
substituted hydroxylamine derivates
-
-
-
sulfonyl fluoride triazine derivates
-
-
sulfonyl fluoride triazine derivates
-
-
sulfonyl fluoride triazine derivates
-
-
sulfonyl fluoride triazine derivates
-
-
sulfonyl fluoride triazine derivates
-
-
sulfonyl fluoride triazine derivates
-
-
tetrahydrofolate
strong substrate inhibition
tetrahydrofolate
-
strong and pH-dependent substrate inhibition due to the formation of the enzyme-glycine:tetrahydrofolate dead-end complex (at low pH values)
tetrahydrofolate
isoform SHMT2 maintains a pronounced tetrahydrofolate substrate inhibition even at the alkaline pH characteristic of the mitochondrial matrix
tetrahydrofolate
inhibitory at non-saturating concentration of serine, at concentrations above 1.5 mM
tetrahydrofolate
at concentrations above 0.015 mM, substrate inhibition is observed
tetrahydrofolate derivatives
-
-
-
tetrahydrofolate derivatives
-
-
-
tetrahydrofolate derivatives
-
-
-
tetrahydrofolate derivatives
-
-
-
tetrahydrofolate derivatives
-
-
-
tetrahydrofolate derivatives
-
-
-
tetrahydrofolate derivatives
-
-
-
Thiosemicarbazide
-
-
Thiosemicarbazide
-
poorly active against promastigotes, but SHMT-S transfectants can provide a small but significant resistance
Urea
in 1 M urea, almost all the cofactor is bound to the enzyme as internal aldimine, indicating that the loss of activity does not result from the denaturation of the active site, these observations suggest that urea might act as an enzyme inhibitor
Urea
81% loss of activity at 1M
Zn2+
2.91% residual activity at 1 mM
additional information
model of uncompetitive substrate inhibition using tetrahydropteroylglutamates with different numbers of glutamate residues, overview
-
additional information
-
model of uncompetitive substrate inhibition using tetrahydropteroylglutamates with different numbers of glutamate residues, overview
-
additional information
-
not: iodoacetate
-
additional information
-
-
-
additional information
-
not: ethanolamine, ethylenediamine; not: valine, leucine, glutamic acid, 3-hydroxybutyric acid
-
additional information
-
not: valine, leucine, glutamic acid, 3-hydroxybutyric acid
-
additional information
the enzyme is not significantly influenced in activity by NH4+, Sl2+, Ca2+, Pb2+, SDS and CTAB
-
additional information
-
the enzyme is not significantly influenced in activity by NH4+, Sl2+, Ca2+, Pb2+, SDS and CTAB
-
additional information
-
not: methionine, S-adenosyl-L-methionine, XMP, IMP, phosphoglycerate
-
additional information
prototypes with negative total charge have greater affinity for Plasmodium falciparum SHMT than for human SHMT
-
additional information
-
not: EDTA
-
additional information
-
inhibition kinetics
-
additional information
-
not: iodoacetate; not: NaN3, mono- or divalent cations, 2-mercaptoethanol, DTT; not: purine nucleoside mono-, di- and triphosphates
-
additional information
-
not: chloroacetamide; not: iodoacetate
-
additional information
-
inhibition kinetics
-
additional information
-
inhibition kinetics
-
additional information
-
not: N-/O-chloroacetyl and N-/O-bromoacetyl derivatives of glycine and L-serine
-
additional information
-
inhibition kinetics
-
additional information
-
in order to act as selective ligands for the active site, the tails of the 5-formyl-6-hydrofolic acid analogues as potential selective inhibitors should be short to avoid the repulsive interactions with residues Lys138, Lys139 and Lys140 of the active site of SHMT, the tails may be longer, but in that case they must possess both negative and positive charges at the right positions, in order to explore their interactions with Lys138, Lys139, Lys140 and Glu137, prototypes with negative total charge have greater affinity for Plasmodium falciparum SHMT than for human SHMT
-
additional information
-
not: mercaptopropionic acid, mercaptoethanolamine; not: valine, leucine, glutamic acid, 3-hydroxybutyric acid
-
additional information
-
not: EDTA; not: purine nucleoside mono-, di- and triphosphates
-
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evolution
-
serine hydroxymethyltransferase is a ubiquitous representative of the family of fold type I pyridoxal 5'-phosphate-dependent enzymes, structural determinants, overview
evolution
-
serine hydroxymethyltransferase is a ubiquitous representative of the family of fold type I pyridoxal 5'-phosphate-dependent enzymes, structural determinants, overview
evolution
SHMT is a ubiquitous enzyme and its sequence and structure were conserved during divergent evolution. SHMT belongs to the fold type-I superfamily of PLP-dependent enzymes, a very complex group of proteins arising from an intricate evolutionary process
evolution
SHMT is a ubiquitous enzyme and its sequence and structure were conserved during divergent evolution. SHMT belongs to the fold type-I superfamily of PLP-dependent enzymes, a very complex group of proteins arising from an intricate evolutionary process
evolution
SHMT is a ubiquitous enzyme and its sequence and structure were conserved during divergent evolution. SHMT belongs to the fold type-I superfamily of PLP-dependent enzymes, a very complex group of proteins arising from an intricate evolutionary process
evolution
SHMT is a ubiquitous enzyme and its sequence and structure were conserved during divergent evolution. SHMT belongs to the fold type-I superfamily of PLP-dependent enzymes, a very complex group of proteins arising from an intricate evolutionary process
evolution
SHMT is a ubiquitous enzyme and its sequence and structure were conserved during divergent evolution. SHMT belongs to the fold type-I superfamily of PLP-dependent enzymes, a very complex group of proteins arising from an intricate evolutionary process
evolution
SHMT is a ubiquitous enzyme and its sequence and structure were conserved during divergent evolution. SHMT belongs to the fold type-I superfamily of PLP-dependent enzymes, a very complex group of proteins arising from an intricate evolutionary process
evolution
SHMT is a ubiquitous enzyme and its sequence and structure were conserved during divergent evolution. SHMT belongs to the fold type-I superfamily of PLP-dependent enzymes, a very complex group of proteins arising from an intricate evolutionary process
evolution
SHMT is a ubiquitous enzyme and its sequence and structure were conserved during divergent evolution. SHMT belongs to the fold type-I superfamily of PLP-dependent enzymes, a very complex group of proteins arising from an intricate evolutionary process
evolution
SHMT is a ubiquitous enzyme and its sequence and structure were conserved during divergent evolution. SHMT belongs to the fold type-I superfamily of PLP-dependent enzymes, a very complex group of proteins arising from an intricate evolutionary process
evolution
SHMT is a ubiquitous enzyme and its sequence and structure were conserved during divergent evolution. SHMT belongs to the fold type-I superfamily of PLP-dependent enzymes, a very complex group of proteins arising from an intricate evolutionary process
evolution
SHMT is a ubiquitous enzyme and its sequence and structure were conserved during divergent evolution. SHMT belongs to the fold type-I superfamily of PLP-dependent enzymes, a very complex group of proteins arising from an intricate evolutionary process
evolution
-
the enzyme belongs to the alpha class of PLP-dependent enzymes. The ligand binding environment of enzymes SHMT from human and Plasmodium are different, overview
evolution
-
the enzyme belongs to the alpha class of PLP-dependent enzymes. The ligand binding environment of enzymes SHMT from human and Plasmodium are different, overview
evolution
the enzyme belongs to the alpha class of PLP-dependent enzymes. The ligand binding environment of enzymes SHMT from human and Plasmodium are different, overview
evolution
-
the enzyme belongs to the alpha-family of fold type I, and pyridoxal 5'-phosphate-dependent enzymes
evolution
the enzyme belongs to the fold type-I superfamily of PLP-dependent enzymes
evolution
-
SHMT is a ubiquitous enzyme and its sequence and structure were conserved during divergent evolution. SHMT belongs to the fold type-I superfamily of PLP-dependent enzymes, a very complex group of proteins arising from an intricate evolutionary process
-
evolution
-
SHMT is a ubiquitous enzyme and its sequence and structure were conserved during divergent evolution. SHMT belongs to the fold type-I superfamily of PLP-dependent enzymes, a very complex group of proteins arising from an intricate evolutionary process
-
evolution
-
the enzyme belongs to the alpha-family of fold type I, and pyridoxal 5'-phosphate-dependent enzymes
-
evolution
-
SHMT is a ubiquitous enzyme and its sequence and structure were conserved during divergent evolution. SHMT belongs to the fold type-I superfamily of PLP-dependent enzymes, a very complex group of proteins arising from an intricate evolutionary process
-
evolution
-
SHMT is a ubiquitous enzyme and its sequence and structure were conserved during divergent evolution. SHMT belongs to the fold type-I superfamily of PLP-dependent enzymes, a very complex group of proteins arising from an intricate evolutionary process
-
evolution
-
SHMT is a ubiquitous enzyme and its sequence and structure were conserved during divergent evolution. SHMT belongs to the fold type-I superfamily of PLP-dependent enzymes, a very complex group of proteins arising from an intricate evolutionary process
-
evolution
-
SHMT is a ubiquitous enzyme and its sequence and structure were conserved during divergent evolution. SHMT belongs to the fold type-I superfamily of PLP-dependent enzymes, a very complex group of proteins arising from an intricate evolutionary process
-
malfunction
-
Shmt1 null mice are fertile and do not demonstrate maternal lethality
malfunction
-
a shm1 null mutant requires CO2-enriched air to inhibit photorespiration, while a shm2 null mutant does not show any visible impairment, a double-null mutant cannot survive in CO2-enriched air. Residual SHM activity is undetectably low in purified leaf mesophyll mitochondria of the shm1 mutant. In roots, the knockout of SHM1 does not reduce total SHM activity, whereas the knockout of SHM2 significantly lowers total SHM activity
malfunction
overexpression of mitochondrial serine hydroxymethyltransferase assures an adequate supply of glycine to rapidly proliferating cancer cells, silencing of mitochondrial serine hydroxymethyltransferase halts cancer cell proliferation and supplementation with sarcosine (a glycine-related metabolite) or formate (a source of one carbon units) fails to rescue cell proliferation
malfunction
suppression of SHMT2 decreases both net serine consumption and glycine production in LN229 cells and completely prevents glycine cleavage activity in isolated mitochondria. The preemptive knockdown of SHMT2 protects BT145, LN229, and U251 cells against the detrimental effects of GLDC knockdown
malfunction
-
a shm1mutant has chlorotic lesions and a considerably smaller, lethal phenotype under natural ambient CO2 concentrations, but can be restored to wild type with normal growth under elevated CO2 levels (0.5% CO2), showing a typical photorespiratory phenotype
malfunction
-
digestion of blood is inhibited in enzyme RNAi-silenced female Aedes aegypti mosquitoes. Enzyme-depleted female mosquitoes lose their flight ability and die within 48 h of a blood meal
malfunction
-
digestion of blood is inhibited in enzyme RNAi-silenced female Aedes aegypti mosquitoes. Enzyme-depleted female mosquitoes lose their flight ability and die within 48 h of a blood meal
-
metabolism
-
SHMT1 is a rate-limiting enzyme in de novo thymidylate biosynthesis
metabolism
-
the enzyme regulates the partitioning of 5,10-methylenetetrahydrofolate between the thymidylate and homocysteine remethylation pathways, mitochondrial SHMT-derived one-carbon units are essential for folate-mediated one-carbon metabolism in the cytoplasm
metabolism
-
the de novo thymidylate biosynthetic pathway forms a multienzyme complex, containing enzymes serine hydroxymethyltransferase 1 and 2alpha, thymidylate synthase, and dihydrofolate reductase, the complex is associated with the nuclear lamina, overview. The de novo thymidylate biosynthetic pathway in mammalian cells translocates to the nucleus for DNA replication and repair. SHMT1 or SHMT2alpha are required for co-localization of dihydrofolate reductase, SHMT, and thymidylate synthase to the nuclear lamina, indicating that SHMT serves as scaffold protein that is essential for complex formation, SHMT1 scaffold function can determine de novo thymidylate synthesis capacity, SHMT1 interaction with TYMS and DHFR is DNA-dependent, but the formation of thymidylate biosynthesis complex is nucleotide-independent. Folate-mediated one-carbon metabolism in the cytoplasm and nucleus, overview
metabolism
-
the reaction catalyzed by this enzyme, the reversible transfer of the Cbeta of serine to tetrahydropteroylglutamate, represents a link between amino acid and folates metabolism and operates as a major source of one-carbon units for several essential biosynthetic processes
metabolism
-
the reaction catalyzed by this enzyme, the reversible transfer of the Cbeta of serine to tetrahydropteroylglutamate, represents a link between amino acid and folates metabolism and operates as a major source of one-carbon units for several essential biosynthetic processes
metabolism
the enzyme plays an essential role in one-carbon unit metabolism
metabolism
key role for serine and glycine metabolism in the survival of brain cancer cells within the ischemic zones of gliomas. Glycine decarboxylase inhibition impairs cells with high SHMT2 levels as the excess glycine not metabolized by glycine decarboxylase can be converted to the toxic molecules aminoacetone and methylglyoxal. SHMT2 activity limits that of pyruvate kinase (PKM2) and reduces oxygen consumption, eliciting a metabolic state that confers a profound survival advantage to cells in poorly vascularized tumor regions
metabolism
the enzyme is involved in folate recycling and dTMP synthesis
metabolism
-
the mitochondrial isoform SHMT2 is a crucial factor in the serine/glycine metabolism in several cancer cell types. Correlation of expression level of SHMT2 and other clinicopathological parameters in clinical breast cancer, overview
metabolism
-
Shm2 is a key enzyme at the crossing point between purine, methionine and folate metabolism
metabolism
-
Shm2 is a key enzyme at the crossing point between purine, methionine and folate metabolism
-
metabolism
-
the enzyme plays an essential role in one-carbon unit metabolism
-
physiological function
-
cytoplasmic serine hydroxymethyltransferase regulates the metabolic partitioning of methylenetetrahydrofolate but is not essential in mice
physiological function
-
the mitochondrial SHMT is required for photorespiration
physiological function
-
the UV-induced increase in SHMT1 translation is accompanied by an increase in the small ubiquitin-like modifier-dependent nuclear localization of the de novo thymidylate biosynthesis pathway and a decrease in DNA strand breaks, suggesting that SHMT1 plays a role in DNA repair
physiological function
-
functional redundancy of SHMT2alpha and SHMT1 in nuclear de novo thymidylate synthesis. The de novo thymidylate biosynthetic pathway forms a multienzyme complex, containing enzymes serine hydroxymethyltransferase 1 and 2alpha, thymidylate synthase, and dihydrofolate reductase, the complex is associated with the nuclear lamina, overview. The de novo thymidylate biosynthetic pathway in mammalian cells translocates to the nucleus for DNA replication and repair. SHMT1 or SHMT2alpha are required for co-localization of dihydrofolate reductase, SHMT, and thymidylate synthase to the nuclear lamina, indicating that SHMT serves as scaffold protein that is essential for complex formation. SHMT expression is rate-limiting for de novo thymidylate synthesis
physiological function
-
in plastids, SHMTs are thought to catalytically direct the hydroxymethyl moiety of serine into the metabolic network of H4PteGlun-bound one-carbon units
physiological function
-
in plastids, SHMTs are thought to catalytically direct the hydroxymethyl moiety of serine into the metabolic network of H4PteGlun-bound one-carbon units
physiological function
in plastids, SHMTs are thought to catalytically direct the hydroxymethyl moiety of serine into the metabolic network of H4PteGlun-bound one-carbon units
physiological function
salt-induced ApSHMT increases the level of glycine betaine via L-serine and choline and confers tolerance to salinity stress
physiological function
-
serine hydroxymethyltransferases are important enzymes of cellular one-carbon metabolism and are essential for the photorespiratory glycine-into-serine conversion in leaf mesophyll mitochondria. SHM1 is the photorespiratory isozyme. Due to exclusion of SHM2 from the photorespiratory environment of mesophyll mitochondria, SHM2 cannot substitute for SHM1 in photorespiratory metabolism. SHM1 and SHM2 operate in a redundant manner in one-carbon metabolism of nonphotorespiring cells with a high demand of one-carbon units, e.g. during lignification of vascular cells, detailed overview
physiological function
-
the enzyme is essential for the acquisition of one-carbon units for subsequent transfer reactions
physiological function
-
the reaction catalyzed by this enzyme, the reversible transfer of the Cbeta of serine to tetrahydropteroylglutamate, represents a link between amino acid and folates metabolism and operates as a major source of one-carbon units for several essential biosynthetic processes, e.g. as a primary source of the one carbon units required for the synthesis of thymidylate, purines, and methionine. SHMT also catalyzes the hydrolysis of 5,10-methenyl-tetrahydropteroylglutamate to 5-formyl-tetrahydropteroylglutamate, which serves as a storage form of reduced folates and one-carbon groups in cells in a dormant stage
physiological function
-
the reaction catalyzed by this enzyme, the reversible transfer of the Cbeta of serine to tetrahydropteroylglutamate, represents a link between amino acid and folates metabolism and operates as a major source of one-carbon units for several essential biosynthetic processes, e.g. as a primary source of the one carbon units required for the synthesis of thymidylate, purines, and methionine. SHMT also catalyzes the hydrolysis of 5,10-methenyl-tetrahydropteroylglutamate to 5-formyl-tetrahydropteroylglutamate,which serves as a storage formof reduced folates and onecarbon groups in cells in a dormant stage
physiological function
mitochondrial serine hydroxymethyltransferase seems to be fundamental to sustain cancer metabolism since production of glycine fuels heme biosynthesis and therefore oxidative phosphorylation. Respiration of cancer cells may then ultimately rely on endogenous glycine synthesis by mitochondrial serine hydroxymethyltransferase. The link between mitochondrial serine hydroxymethyltransferase activity and heme biosynthesis represents an important aspect of cancer cell metabolism. Glycine itself, rather than one-carbon units deriving from the SHMT2 reaction, is specifically critical in cancer cells
physiological function
-
SHMT plays an important role in the assimilation of C1 compounds, yielding the main L-serine intermediate
physiological function
SHMT2 is required for cancer cells to adapt to the tumor environment, but also renders these cells sensitive to glycine cleavage system inhibition. The enzyme has a key role in cells in environments with limited oxygen or nutrient levels
physiological function
SHMTs are an important group of pyridoxal-5'-phosphate-dependent enzymes that catalyze the reversible conversion of L-serine and tetrahydropteroylglutamate to glycine and 5,10-methylenetetrahydropteroylglutamate. The enzyme plays a central role in one-carbon unit metabolism
physiological function
SHMTs are an important group of pyridoxal-5'-phosphate-dependent enzymes that catalyze the reversible conversion of L-serine and tetrahydropteroylglutamate to glycine and 5,10-methylenetetrahydropteroylglutamate. The enzyme plays a central role in one-carbon unit metabolism. SHMT also catalyzes the 5,10-methylenetetrahydropteroylglutamate-independent cleavage of many 3-hydroxyamino acids and the decarboxylation of aminomalonate, at rates similar to that of H4PteGlu-dependent serine cleavage
physiological function
SHMTs are an important group of pyridoxal-5'-phosphate-dependent enzymes that catalyze the reversible conversion of L-serine and tetrahydropteroylglutamate to glycine and 5,10-methylenetetrahydropteroylglutamate. The enzyme plays a central role in one-carbon unit metabolism. SHMT also catalyzes the H4PteGlu-independent cleavage of many 3-hydroxyamino acids and the decarboxylation of aminomalonate, at rates similar to that of H4PteGlu-dependent serine cleavage
physiological function
SHMTs are an important group of pyridoxal-5'-phosphate-dependent enzymes that catalyze the reversible conversion of L-serine and tetrahydropteroylglutamate to glycine and 5,10-methylenetetrahydropteroylglutamate. The enzyme plays a central role in one-carbon unit metabolism. SHMT also catalyzes the H4PteGlu-independent cleavage of many 3-hydroxyamino acids and the decarboxylation of aminomalonate, at rates similar to that of H4PteGlu-dependent serine cleavage
physiological function
SHMTs are an important group of pyridoxal-5'-phosphate-dependent enzymes that catalyze the reversible conversion of L-serine and tetrahydropteroylglutamate to glycine and 5,10-methylenetetrahydropteroylglutamate. The enzyme plays a central role in one-carbon unit metabolism. SHMT also catalyzes the H4PteGlu-independent cleavage of many 3-hydroxyamino acids and the decarboxylation of aminomalonate, at rates similar to that of H4PteGlu-dependent serine cleavage
physiological function
SHMTs are an important group of pyridoxal-5'-phosphate-dependent enzymes that catalyze the reversible conversion of L-serine and tetrahydropteroylglutamate to glycine and 5,10-methylenetetrahydropteroylglutamate. The enzyme plays a central role in one-carbon unit metabolism. SHMT also catalyzes the H4PteGlu-independent cleavage of many 3-hydroxyamino acids and the decarboxylation of aminomalonate, at rates similar to that of H4PteGlu-dependent serine cleavage
physiological function
SHMTs are an important group of pyridoxal-5'-phosphate-dependent enzymes that catalyze the reversible conversion of L-serine and tetrahydropteroylglutamate to glycine and 5,10-methylenetetrahydropteroylglutamate. The enzyme plays a central role in one-carbon unit metabolism. SHMT also catalyzes the H4PteGlu-independent cleavage of many 3-hydroxyamino acids and the decarboxylation of aminomalonate, at rates similar to that of H4PteGlu-dependent serine cleavage
physiological function
SHMTs are an important group of pyridoxal-5'-phosphate-dependent enzymes that catalyze the reversible conversion of L-serine and tetrahydropteroylglutamate to glycine and 5,10-methylenetetrahydropteroylglutamate. The enzyme plays a central role in one-carbon unit metabolism. SHMT also catalyzes the H4PteGlu-independent cleavage of many 3-hydroxyamino acids and the decarboxylation of aminomalonate, at rates similar to that of H4PteGlu-dependent serine cleavage
physiological function
SHMTs are an important group of pyridoxal-5'-phosphate-dependent enzymes that catalyze the reversible conversion of L-serine and tetrahydropteroylglutamate to glycine and 5,10-methylenetetrahydropteroylglutamate. The enzyme plays a central role in one-carbon unit metabolism. SHMT also catalyzes the H4PteGlu-independent cleavage of many 3-hydroxyamino acids and the decarboxylation of aminomalonate, at rates similar to that of H4PteGlu-dependent serine cleavage
physiological function
SHMTs are an important group of pyridoxal-5'-phosphate-dependent enzymes that catalyze the reversible conversion of L-serine and tetrahydropteroylglutamate to glycine and 5,10-methylenetetrahydropteroylglutamate. The enzyme plays a central role in one-carbon unit metabolism. SHMT also catalyzes the H4PteGlu-independent cleavage of many 3-hydroxyamino acids and the decarboxylation of aminomalonate, at rates similar to that of H4PteGlu-dependent serine cleavage
physiological function
SHMTs are an important group of pyridoxal-5'-phosphate-dependent enzymes that catalyze the reversible conversion of L-serine and tetrahydropteroylglutamate to glycine and 5,10-methylenetetrahydropteroylglutamate. The enzyme plays a central role in one-carbon unit metabolism. SHMT also catalyzes the H4PteGlu-independent cleavage of many 3-hydroxyamino acids and the decarboxylation of aminomalonate, at rates similar to that of H4PteGlu-dependent serine cleavage
physiological function
SHMTs are an important group of pyridoxal-5'-phosphate-dependent enzymes that catalyze the reversible conversion of L-serine and tetrahydropteroylglutamate to glycine and 5,10-methylenetetrahydropteroylglutamate. The enzyme plays a central role in one-carbon unit metabolism. SHMT also catalyzes the H4PteGlu-independent cleavage of many 3-hydroxyamino acids and the decarboxylation of aminomalonate, at rates similar to that of H4PteGlu-dependent serine cleavage
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
physiological function
-
the enzyme is essential for parasite viability
physiological function
-
the enzyme is essential for parasite viability
physiological function
-
Synechococcus elongatus PCC7942 cells expressing the enzyme from Aphanothece halophytica reveal an increase in growth under salt stress condition
physiological function
the enzyme dynamically changes the fluxes of one-carbon metabolism by reversibly converting L-serine and tetrahydrofolate into 5,10-methylene-tetrahydrofolate and glycine. The cytosolic isoforms can also translocate to the nucleus to sustain de novo thymidylate synthesis and support cell proliferation
physiological function
-
the enzyme has additional functions aside from its main enzymatic role in soybean cyst nematode resistance
physiological function
-
SHMTs are an important group of pyridoxal-5'-phosphate-dependent enzymes that catalyze the reversible conversion of L-serine and tetrahydropteroylglutamate to glycine and 5,10-methylenetetrahydropteroylglutamate. The enzyme plays a central role in one-carbon unit metabolism. SHMT also catalyzes the H4PteGlu-independent cleavage of many 3-hydroxyamino acids and the decarboxylation of aminomalonate, at rates similar to that of H4PteGlu-dependent serine cleavage
-
physiological function
-
in plastids, SHMTs are thought to catalytically direct the hydroxymethyl moiety of serine into the metabolic network of H4PteGlun-bound one-carbon units
-
physiological function
-
in plastids, SHMTs are thought to catalytically direct the hydroxymethyl moiety of serine into the metabolic network of H4PteGlun-bound one-carbon units
-
physiological function
-
SHMTs are an important group of pyridoxal-5'-phosphate-dependent enzymes that catalyze the reversible conversion of L-serine and tetrahydropteroylglutamate to glycine and 5,10-methylenetetrahydropteroylglutamate. The enzyme plays a central role in one-carbon unit metabolism. SHMT also catalyzes the H4PteGlu-independent cleavage of many 3-hydroxyamino acids and the decarboxylation of aminomalonate, at rates similar to that of H4PteGlu-dependent serine cleavage
-
physiological function
-
SHMT plays an important role in the assimilation of C1 compounds, yielding the main L-serine intermediate
-
physiological function
-
SHMTs are an important group of pyridoxal-5'-phosphate-dependent enzymes that catalyze the reversible conversion of L-serine and tetrahydropteroylglutamate to glycine and 5,10-methylenetetrahydropteroylglutamate. The enzyme plays a central role in one-carbon unit metabolism. SHMT also catalyzes the H4PteGlu-independent cleavage of many 3-hydroxyamino acids and the decarboxylation of aminomalonate, at rates similar to that of H4PteGlu-dependent serine cleavage
-
physiological function
-
SHMTs are an important group of pyridoxal-5'-phosphate-dependent enzymes that catalyze the reversible conversion of L-serine and tetrahydropteroylglutamate to glycine and 5,10-methylenetetrahydropteroylglutamate. The enzyme plays a central role in one-carbon unit metabolism. SHMT also catalyzes the H4PteGlu-independent cleavage of many 3-hydroxyamino acids and the decarboxylation of aminomalonate, at rates similar to that of H4PteGlu-dependent serine cleavage
-
physiological function
-
SHMTs are an important group of pyridoxal-5'-phosphate-dependent enzymes that catalyze the reversible conversion of L-serine and tetrahydropteroylglutamate to glycine and 5,10-methylenetetrahydropteroylglutamate. The enzyme plays a central role in one-carbon unit metabolism. SHMT also catalyzes the H4PteGlu-independent cleavage of many 3-hydroxyamino acids and the decarboxylation of aminomalonate, at rates similar to that of H4PteGlu-dependent serine cleavage
-
physiological function
-
SHMTs are an important group of pyridoxal-5'-phosphate-dependent enzymes that catalyze the reversible conversion of L-serine and tetrahydropteroylglutamate to glycine and 5,10-methylenetetrahydropteroylglutamate. The enzyme plays a central role in one-carbon unit metabolism. SHMT also catalyzes the H4PteGlu-independent cleavage of many 3-hydroxyamino acids and the decarboxylation of aminomalonate, at rates similar to that of H4PteGlu-dependent serine cleavage
-
additional information
amino acid residues important for the structure and function of SHMT are Y56, D202, and K231 for the interaction with pyridoxal 5'-phosphate, R64 and D73 for inter-subunit interaction, H127 for cofactor binding, and P258 and R363 for substrate interaction
additional information
-
amino acid residues important for the structure and function of SHMT are Y56, D202, and K231 for the interaction with pyridoxal 5'-phosphate, R64 and D73 for inter-subunit interaction, H127 for cofactor binding, and P258 and R363 for substrate interaction
additional information
-
both PfSHMTc and PfSHMTm show dynamic, stage-dependent localization among the different compartments of the parasite and sequence analysis suggests they may also reversibly associate with each other, a factor that may be critical to folate cofactor function, given the apparent lack of enzymic activity of PfSHMTm
additional information
-
kinetic properties of SHM2 might render this enzyme unsuitable for the high-folate conditions of photorespiring mesophyll mitochondria
additional information
analysis of buried water clusters in the inner region of the SHMT dimers using the enzyme crystal structure, PDB 1DFO, molecular dynamics, overview
additional information
analysis of buried water clusters in the inner region of the SHMT dimers using the enzyme crystal structure, PDB 1KKJ, molecular dynamics, overview
additional information
analysis of buried water clusters in the inner region of the SHMT dimers using the enzyme crystal structure, PDB 2DKJ, molecular dynamics, overview
additional information
analysis of buried water clusters in the inner region of the SHMT dimers using the enzyme crystal structure, PDB 3ECD, molecular dynamics, overview
additional information
analysis of buried water clusters in the inner region of the SHMT dimers using the enzyme crystal structure, PDB 3GBX, molecular dynamics, overview
additional information
analysis of buried water clusters in the inner region of the SHMT dimers using the enzyme crystal structure, PDB 3H7F, molecular dynamics, overview
additional information
analysis of buried water clusters in the inner region of the SHMT dimers using the enzyme crystal structure, PDB 3N0L, molecular dynamics, overview
additional information
analysis of buried water clusters in the inner region of the SHMT dimers using the enzyme crystal structure, PDB 3PGY, molecular dynamics, overview
additional information
analysis of buried water clusters in the inner region of the SHMT dimers using the enzyme crystal structure, PDB 4J5U, molecular dynamics, overview
additional information
analysis of buried water clusters in the inner region of the SHMT dimers using the enzyme crystal structure, PDB 4N0W, molecular dynamics, overview
additional information
analysis of buried water clusters in the inner region of the SHMT dimers using the enzyme crystal structure, PDB 4P3M, molecular dynamics, overview
additional information
the enzyme psychrophilic shows high catalytic activity at low temperature and thermolability, three-dimensional structure analysis and structure-function relationship, homology modeling of the holoenzyme form, overview. The apoform enzyme is in an open conformation and possesses four or five (in chain A) disordered loops that interact with the cofactor. Cofactor binding triggers a rearrangement of the small domain that moves toward the large domain and screens the pyridoxal 5'-phosphate binding site at the solvent side
additional information
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the enzyme psychrophilic shows high catalytic activity at low temperature and thermolability, three-dimensional structure analysis and structure-function relationship, homology modeling of the holoenzyme form, overview. The apoform enzyme is in an open conformation and possesses four or five (in chain A) disordered loops that interact with the cofactor. Cofactor binding triggers a rearrangement of the small domain that moves toward the large domain and screens the pyridoxal 5'-phosphate binding site at the solvent side
additional information
-
analysis of buried water clusters in the inner region of the SHMT dimers using the enzyme crystal structure, PDB 3N0L, molecular dynamics, overview
-
additional information
-
analysis of buried water clusters in the inner region of the SHMT dimers using the enzyme crystal structure, PDB 4P3M, molecular dynamics, overview
-
additional information
-
analysis of buried water clusters in the inner region of the SHMT dimers using the enzyme crystal structure, PDB 3H7F, molecular dynamics, overview
-
additional information
-
analysis of buried water clusters in the inner region of the SHMT dimers using the enzyme crystal structure, PDB 3PGY, molecular dynamics, overview
-
additional information
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analysis of buried water clusters in the inner region of the SHMT dimers using the enzyme crystal structure, PDB 3ECD, molecular dynamics, overview
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additional information
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analysis of buried water clusters in the inner region of the SHMT dimers using the enzyme crystal structure, PDB 4J5U, molecular dynamics, overview
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