Any feedback?
Information on EC 2.1.2.1 - glycine hydroxymethyltransferase and Organism(s) Arabidopsis thaliana and UniProt Accession Q9FPH3
for references in articles please use BRENDA:EC2.1.2.1Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
2.1.2.1 glycine hydroxymethyltransferaseIUBMB Comments
A pyridoxal-phosphate protein. Also catalyses the reaction of glycine with acetaldehyde to form L-threonine, and with 4-trimethylammoniobutanal to form 3-hydroxy-N6,N6,N6-trimethyl-L-lysine.
Specify your search results
Word Map
- 2.1.2.1
-
one-carbon
- pyridoxal
- thymidylate
- purine
- 5'-phosphate
- homocysteine
- dihydrofolate
-
folate-dependent
-
photorespiratory
-
photorespiration
-
folate-mediated
- pyridoxal-5'-phosphate
- thf
- dtmp
- mthfd1
-
plp-dependent
-
remethylation
-
aldimine
- phgdh
- medicine
-
folate-metabolizing
- 5,10-methenyltetrahydrofolate
-
5'-phosphate-dependent
- antifolate
- hydroxypyruvate
-
quinonoid
- 5-methyltetrahydrofolate
- glycerate
- 5-formyltetrahydrofolate
- drug development
-
folate-related
- d-alanine
-
c1-tetrahydrofolate
-
1-carbon
-
5-formyl
- polyglutamate
- l-threonine
-
alpha-protons
-
slc19a1
-
retro-aldol
- degradation
- analysis
- synthesis
- biotechnology
- pharmacology
The taxonomic range for the selected organisms is: Arabidopsis thaliana
The enzyme appears in selected viruses and cellular organisms
The enzyme appears in selected viruses and cellular organisms
Synonyms
serine hydroxymethyltransferase, shmt2, shmt1, serine hydroxymethyl transferase, serine transhydroxymethylase, serine hydroxymethyltransferase 2, mitochondrial serine hydroxymethyltransferase, serine hydroxymethyltransferase 1, bsshmt, pvshmt, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
L-serine hydroxymethyltransferase
-
-
-
-
serine hydroxymethylase hydroxymethyltransferase, serine
-
-
-
-
serine hydroxymethyltransferase
serine transhydroxymethylase
-
-
-
-
SHMT
serine hydroxymethyltransferase
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydroxymethyl group transfer
-
-
-
-
PATHWAY SOURCE
PATHWAYS
KEGG
-
-, -, -, -, -, -, -, -, -, -, -, -, -, -
SYSTEMATIC NAME
IUBMB Comments
5,10-methylenetetrahydrofolate:glycine hydroxymethyltransferase
A pyridoxal-phosphate protein. Also catalyses the reaction of glycine with acetaldehyde to form L-threonine, and with 4-trimethylammoniobutanal to form 3-hydroxy-N6,N6,N6-trimethyl-L-lysine.
CAS REGISTRY NUMBER
COMMENTARY
9029-83-8
-
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
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
L-serine + tetrahydrofolate
glycine + 5,10-methylenetetrahydrofolate + H2O
-
-
-
-
?
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
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
5,10-methylenetetrahydrofolate + glycine + H2O
tetrahydrofolate + L-serine
-
-
-
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
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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
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
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.2177
tetrahydrofolate
pH 8.5, temperature not specified in the publication, recombinant AtSHMT3
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
15.8
tetrahydrofolate
pH 8.5, temperature not specified in the publication, recombinant AtSHMT3
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
70
tetrahydrofolate
pH 8.5, temperature not specified in the publication, recombinant AtSHMT3
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.085
tetrahydropteroylglutamate
pH 8.5, temperature not specified in the publication, recombinant AtSHMT3
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
additional information
-
cellular distribution of SHM1 and SHM2, detailed overview
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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
physiological function
additional information
-
kinetic properties of SHM2 might render this enzyme unsuitable for the high-folate conditions of photorespiring mesophyll mitochondria
physiological function
-
the mitochondrial SHMT is required for photorespiration
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
-
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
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
-
5-CHO-THF cycloligase mutant, doubled leaf 5-formyltetrahydrofolate level, little impact on SHMT activity, but glycine content of mutant leaves is 19fold higher than the wild-type, also a small accumulation of serine in the mutant relative to the wild-type
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
phylogenetic analysis, expression in Escherichia coli strain Rosetta, transient expression of EGFP-tagged full-length AtSHMT3 in Arabidopsis thaliana leaf protoplasts
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
in mitochondria, ferredoxin-dependent glutamate synthase interacts physically with SHMT1, and this interaction is necessary for photorespiratory SHMT activity
-
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Moreno, J.I.; Martin, R.; Castresana, C.
Arabidopsis SHMT1, a serine hydroxymethyltransferase that functions in the photorespiratory pathway influences resistance to biotic and abiotic stress
Plant J.
41
451-463
2005
Arabidopsis thaliana, Arabidopsis thaliana C24
Goyer, A.; Collakova, E.; Diaz de la Garza, R.; Quinlivan, E.P.; Williamson, J.; Gregory, J.F., 3rd; Shachar-Hill, Y.; Hanson, A.D.
5-Formyltetrahydrofolate is an inhibitory but well tolerated metabolite in Arabidopsis leaves
J. Biol. Chem.
280
26137-26142
2005
Arabidopsis thaliana
Jamai, A.; Salome, P.A.; Schilling, S.H.; Weber, A.P.; McClung, C.R.
Arabidopsis photorespiratory serine hydroxymethyltransferase activity requires the mitochondrial accumulation of ferredoxin-dependent glutamate synthase
Plant Cell
21
595-606
2009
Arabidopsis thaliana
Zhang, Y.; Sun, K.; Sandoval, F.J.; Santiago, K.; Roje, S.
One-carbon metabolism in plants: characterization of a plastid serine hydroxymethyltransferase
Biochem. J.
430
97-105
2010
Hordeum vulgare, Pisum sativum, Arabidopsis thaliana (Q94JQ3), Arabidopsis thaliana, Hordeum vulgare Bob, Pisum sativum Progress 9
EXTERNAL LINKS (specific for EC-Number 2.1.2.1)
Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.
Release 2023.1 (January 2023)
Legal
Curated at
Member of
