Information on EC 2.1.2.1 - glycine hydroxymethyltransferase

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The expected taxonomic range for this enzyme is: Archaea, Bacteria, Eukaryota

EC NUMBER
COMMENTARY
2.1.2.1
-
RECOMMENDED NAME
GeneOntology No.
glycine hydroxymethyltransferase
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
5,10-methylenetetrahydrofolate + glycine + H2O = tetrahydrofolate + L-serine
show the reaction diagram
mechanism
-
5,10-methylenetetrahydrofolate + glycine + H2O = tetrahydrofolate + L-serine
show the reaction diagram
mechanism
-
5,10-methylenetetrahydrofolate + glycine + H2O = tetrahydrofolate + L-serine
show the reaction diagram
mechanism
-
5,10-methylenetetrahydrofolate + glycine + H2O = tetrahydrofolate + L-serine
show the reaction diagram
mechanism
-
5,10-methylenetetrahydrofolate + glycine + H2O = tetrahydrofolate + L-serine
show the reaction diagram
mechanism
-
5,10-methylenetetrahydrofolate + glycine + H2O = tetrahydrofolate + L-serine
show the reaction diagram
mechanism
-
5,10-methylenetetrahydrofolate + glycine + H2O = tetrahydrofolate + L-serine
show the reaction diagram
mechanism
-
5,10-methylenetetrahydrofolate + glycine + H2O = tetrahydrofolate + L-serine
show the reaction diagram
mechanism
-
5,10-methylenetetrahydrofolate + glycine + H2O = tetrahydrofolate + L-serine
show the reaction diagram
mechanism
-
5,10-methylenetetrahydrofolate + glycine + H2O = tetrahydrofolate + L-serine
show the reaction diagram
mechanism
-
5,10-methylenetetrahydrofolate + glycine + H2O = tetrahydrofolate + L-serine
show the reaction diagram
mechanism
-
5,10-methylenetetrahydrofolate + glycine + H2O = tetrahydrofolate + L-serine
show the reaction diagram
mechanism
-
5,10-methylenetetrahydrofolate + glycine + H2O = tetrahydrofolate + L-serine
show the reaction diagram
stereochemistry
-
5,10-methylenetetrahydrofolate + glycine + H2O = tetrahydrofolate + L-serine
show the reaction diagram
stereochemistry
-
5,10-methylenetetrahydrofolate + glycine + H2O = tetrahydrofolate + L-serine
show the reaction diagram
stereochemistry
-
5,10-methylenetetrahydrofolate + glycine + H2O = tetrahydrofolate + L-serine
show the reaction diagram
stereochemistry
-
5,10-methylenetetrahydrofolate + glycine + H2O = tetrahydrofolate + L-serine
show the reaction diagram
enzyme exhibits threonine aldolase activity (EC 4.1.2.5), but the two enzymes are distinct
-
5,10-methylenetetrahydrofolate + glycine + H2O = tetrahydrofolate + L-serine
show the reaction diagram
evidence for a direct transfer mechanism for the enzyme catalysed reaction
-
5,10-methylenetetrahydrofolate + glycine + H2O = tetrahydrofolate + L-serine
show the reaction diagram
general mechanism of pyridoxal 5'-phosphate-catalyzed aldolic cleavage, racemisation, and transamination reactions, and catalytic mechanism of the transaldimination reaction involving Tyr55, His228, and Arg235, overview. Tyr55 is contributed by the symmetry-related monomer, with respect to the pyridoxal 5'-phosphate-binding subunit, and functions as the general acid-base catalyst in this proton transfer
-
5,10-methylenetetrahydrofolate + glycine + H2O = tetrahydrofolate + L-serine
show the reaction diagram
mechanism
Glycine max L.
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydroxymethyl group transfer
-
-
-
-
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Biosynthesis of antibiotics
-
-
Biosynthesis of secondary metabolites
-
-
Cyanoamino acid metabolism
-
-
folate polyglutamylation
-
-
folate polyglutamylation
-
-
folate transformations I
-
-
folate transformations II
-
-
formaldehyde assimilation I (serine pathway)
-
-
glycine betaine degradation I
-
-
glycine betaine degradation II (mammalian)
-
-
glycine biosynthesis I
-
-
glycine metabolism
-
-
Glycine, serine and threonine metabolism
-
-
Glyoxylate and dicarboxylate metabolism
-
-
Metabolic pathways
-
-
Methane metabolism
-
-
Microbial metabolism in diverse environments
-
-
N10-formyl-tetrahydrofolate biosynthesis
-
-
One carbon pool by folate
-
-
photorespiration
-
-
purine metabolism
-
-
purine nucleobases degradation II (anaerobic)
-
-
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.
SYNONYMS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
L-serine hydroxymethyltransferase
-
-
-
-
serine hydroxymethylase hydroxymethyltransferase, serine
-
-
-
-
serine hydroxymethyltransferase
-
-
-
-
serine transhydroxymethylase
-
-
-
-
CAS REGISTRY NUMBER
COMMENTARY
9029-83-8
-
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
ecotype Columbia
UniProt
Manually annotated by BRENDA team
Arabidopsis thaliana C24
C24
-
-
Manually annotated by BRENDA team
strain ATCC 13032
-
-
Manually annotated by BRENDA team
strain ATCC13032
-
-
Manually annotated by BRENDA team
Corynebacterium glutamicum ATCC13032
strain ATCC13032
-
-
Manually annotated by BRENDA team
AB strain
SwissProt
Manually annotated by BRENDA team
Danio rerio AB
AB strain
SwissProt
Manually annotated by BRENDA team
strain AB90054
-
-
Manually annotated by BRENDA team
Escherichia coli AB90054
strain AB90054
-
-
Manually annotated by BRENDA team
Escherichia coli K-12 MG1655
-
-
-
Manually annotated by BRENDA team
Euglena gracilis Z
-
-
-
Manually annotated by BRENDA team
strain L. Merr. cv. Williams, soybean
-
-
Manually annotated by BRENDA team
Glycine max L.
strain L. Merr. cv. Williams, soybean
-
-
Manually annotated by BRENDA team
Hordeum vulgare Bob
-
-
-
Manually annotated by BRENDA team
strain GM2, a glycine resistant mutant derived from strain KM146
-
-
Manually annotated by BRENDA team
; strain MHOM/IN/80/Dd8
SwissProt
Manually annotated by BRENDA team
Leishmania donovani MHOM/IN/80/Dd8
strain MHOM/IN/80/Dd8
SwissProt
Manually annotated by BRENDA team
Bonnet monkey
-
-
Manually annotated by BRENDA team
Methanosarcina barkeri DSM 804
-
SwissProt
Manually annotated by BRENDA team
Methanospirillum hungatei GP1
-
-
-
Manually annotated by BRENDA team
Pisum sativum Progress 9
-
-
-
Manually annotated by BRENDA team
one enzymatically functional SHMT isozyme, PfSHMTc, and one related, apparently inactive isoform, PfSHMTm, encoded by different genes pfshmt and PF14_ 0534, respectively
-
-
Manually annotated by BRENDA team
Plasmodium falciparum strainTM4
strainTM4
-
-
Manually annotated by BRENDA team
putative
UniProt
Manually annotated by BRENDA team
Wistar strain
-
-
Manually annotated by BRENDA team
Rattus norvegicus Wistar
Wistar strain
-
-
Manually annotated by BRENDA team
strain 3701B
-
-
Manually annotated by BRENDA team
Saccharomyces cerevisiae 3701B
strain 3701B
-
-
Manually annotated by BRENDA team
strain ATCC VR1471
SwissProt
Manually annotated by BRENDA team
cv. Solara, antisense lines G310-10, G310-16, G310-76, G310-101 and G310-106
-
-
Manually annotated by BRENDA team
strain PCC 6803
-
-
Manually annotated by BRENDA team
strains T1 and G3
-
-
Manually annotated by BRENDA team
mung bean
-
-
Manually annotated by BRENDA team
strain ATCC 1470
SwissProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
-
serine hydroxymethyltransferase is a ubiquitous representative of the family of fold type I pyridoxal 5'-phosphate-dependent enzymes, structural determinants, overview
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
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
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
Q94JQ3
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
I7H6W6
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
Hordeum vulgare Bob, Pisum sativum Progress 9
-
in plastids, SHMTs are thought to catalytically direct the hydroxymethyl moiety of serine into the metabolic network of H4PteGlun-bound one-carbon units
-
metabolism
Q58992
the enzyme plays an essential role in one-carbon unit metabolism
additional information
I7H6W6
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
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
(6S)-tetrahydrofolate + L-serine
5,10-methylenetetrahydrofolate + glycine + H2O
show the reaction diagram
Methanosarcina barkeri, Methanosarcina barkeri DSM 804
Q46A52
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
-
-
?
5,10-methenyl-tetrahydropteroyl pentaglutamate + glycine + H2O
5-formyl-tetrahydropteroyl pentaglutamate + L-serine
show the reaction diagram
-
-
-
-
?
5,10-methylenetetrahydrofolate + glycine + H2O
tetrahydrofolate + L-Ser
show the reaction diagram
-
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
show the reaction diagram
-
-
-
-
?
5,10-methylenetetrahydrofolate + glycine + H2O
tetrahydrofolate + L-serine
show the reaction diagram
-
-
-
-
r
5,10-methylenetetrahydrofolate + glycine + H2O
tetrahydrofolate + L-serine
show the reaction diagram
-
-
-
-
?
5,10-methylenetetrahydrofolate + glycine + H2O
tetrahydrofolate + L-serine
show the reaction diagram
-
-
-
-
r
5,10-methylenetetrahydrofolate + glycine + H2O
tetrahydrofolate + L-serine
show the reaction diagram
-
-
-
-
?
5,10-methylenetetrahydrofolate + glycine + H2O
tetrahydrofolate + L-serine
show the reaction diagram
-
-
-
-
?
5,10-methylenetetrahydrofolate + glycine + H2O
tetrahydrofolate + L-serine
show the reaction diagram
Q86LS9
-
-
-
r
5,10-methylenetetrahydrofolate + glycine + H2O
tetrahydrofolate + L-serine
show the reaction diagram
A9LDD9, Q7SXN1
-
-
-
r
5,10-methylenetetrahydrofolate + glycine + H2O
tetrahydrofolate + L-serine
show the reaction diagram
I7H6W6
-
-
-
r
5,10-methylenetetrahydrofolate + glycine + H2O
tetrahydrofolate + L-serine
show the reaction diagram
Q94JQ3
-
-
-
r
5,10-methylenetetrahydrofolate + glycine + H2O
tetrahydrofolate + L-serine
show the reaction diagram
Q94JQ3
-
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
show the reaction diagram
-
tetrahydrofolate-dependent SHMT activity, modeling of substrate binding, overview
-
-
?
5,10-methylenetetrahydrofolate + glycine + H2O
tetrahydrofolate + L-serine
show the reaction diagram
Leishmania donovani MHOM/IN/80/Dd8
Q86LS9
-
-
-
r
5,10-methylenetetrahydrofolate + glycine + H2O
tetrahydrofolate + L-serine
show the reaction diagram
Hordeum vulgare Bob, Pisum sativum Progress 9
-
-
-
-
r
5,10-methylenetetrahydrofolate + glycine + H2O
tetrahydrofolate + L-serine
show the reaction diagram
-
tetrahydrofolate-dependent SHMT activity, modeling of substrate binding, overview
-
-
?
5,6,7,8-tetrahydrofolate + L-Ser
5,10-methylenetetrahydrofolate + glycine + H2O
show the reaction diagram
-
-
-
-
r
alpha-methylserine + tetrahydrofolate
D-alanine + 5,10-methylenetetrahydrofolate
show the reaction diagram
-
-
-
?
alpha-methylserine + tetrahydrofolate
D-alanine + 5,10-methylenetetrahydrofolate
show the reaction diagram
-
-
-
?
alpha-methylserine + tetrahydrofolate
D-alanine + 5,10-methylenetetrahydrofolate
show the reaction diagram
-
-
-
-
?
alpha-methylserine + tetrahydrofolate
D-alanine + 5,10-methylenetetrahydrofolate
show the reaction diagram
-
-
-
-
?
alpha-methylserine + tetrahydrofolate
D-alanine + 5,10-methylenetetrahydrofolate
show the reaction diagram
-
-
-
-
?
alpha-methylserine + tetrahydrofolate
D-alanine + 5,10-methylenetetrahydrofolate
show the reaction diagram
-
-
-
?
alpha-methylserine + tetrahydrofolate
D-alanine + 5,10-methylenetetrahydrofolate
show the reaction diagram
-
-
-
?
alpha-methylserine + tetrahydrofolate
D-alanine + 5,10-methylenetetrahydrofolate
show the reaction diagram
-
-
-
?
alpha-methylserine + tetrahydrofolate
D-alanine + 5,10-methylenetetrahydrofolate
show the reaction diagram
-
-
-
?
alpha-methylserine + tetrahydrofolate
D-alanine + 5,10-methylenetetrahydrofolate
show the reaction diagram
-
-
-
?
alpha-methylserine + tetrahydrofolate
D-alanine + 5,10-methylenetetrahydrofolate
show the reaction diagram
-
-
-
?
alpha-methylserine + tetrahydrofolate
D-alanine + 5,10-methylenetetrahydrofolate
show the reaction diagram
-
-
-
?
alpha-methylserine + tetrahydrofolate
D-alanine + 5,10-methylenetetrahydrofolate
show the reaction diagram
-
-
-
?
alpha-methylserine + tetrahydrofolate
D-alanine + 5,10-methylenetetrahydrofolate
show the reaction diagram
-
-
-
-
?
alpha-methylserine + tetrahydrofolate
D-alanine + 5,10-methylenetetrahydrofolate
show the reaction diagram
-
at high concentrations of enzyme
-
?
D-serine + tetrahydrofolate
glycine + 5,10-methylenetetrahydrofolate + H2O
show the reaction diagram
-
the binding affinity for D-serine is 150fold lower than that of L-serine
-
-
?
D-serine + tetrahydrofolate
glycine + 5,10-methylenetetrahydrofolate + H2O
show the reaction diagram
Plasmodium falciparum, Plasmodium falciparum strainTM4
-
the catalytic efficiency for D-serine is 580fold lower than that of L-serine
-
-
?
L-Ser + tetrahydrofolate
Gly + 5,10-methylenetetrahydrofolate
show the reaction diagram
-
-
-
-
r
L-Ser + tetrahydrofolate
Gly + 5,10-methylenetetrahydrofolate
show the reaction diagram
P07511
-
-
-
?
L-Ser + tetrahydrofolate
Gly + 5,10-methylenetetrahydrofolate
show the reaction diagram
-
-
-
-
?
L-Ser + tetrahydrofolate
Gly + 5,10-methylenetetrahydrofolate
show the reaction diagram
-
-
-
-
?
L-Ser + tetrahydrofolate
Gly + 5,10-methylenetetrahydrofolate
show the reaction diagram
-
placental conversion of serine to glycine is a major source of fetal glycine
-
-
?
L-serine + modified folate
glycine + modified methylenefolate
show the reaction diagram
-
not: tetrahydrofolate, synthetic modified folate derivate
-
?
L-serine + tetrahydrofolate
glycine + 5,10-methylenetetrahydrofolate + H2O
show the reaction diagram
-
-
-
-
L-serine + tetrahydrofolate
glycine + 5,10-methylenetetrahydrofolate + H2O
show the reaction diagram
-
-
-
-
L-serine + tetrahydrofolate
glycine + 5,10-methylenetetrahydrofolate + H2O
show the reaction diagram
-
-
-
-
?
L-serine + tetrahydrofolate
glycine + 5,10-methylenetetrahydrofolate + H2O
show the reaction diagram
-
-
-
?
L-serine + tetrahydrofolate
glycine + 5,10-methylenetetrahydrofolate + H2O
show the reaction diagram
-
-
-
-
r
L-serine + tetrahydrofolate
glycine + 5,10-methylenetetrahydrofolate + H2O
show the reaction diagram
-
-
-
-
L-serine + tetrahydrofolate
glycine + 5,10-methylenetetrahydrofolate + H2O
show the reaction diagram
-
-
-
-
?
L-serine + tetrahydrofolate
glycine + 5,10-methylenetetrahydrofolate + H2O
show the reaction diagram
-
-
-
-
r
L-serine + tetrahydrofolate
glycine + 5,10-methylenetetrahydrofolate + H2O
show the reaction diagram
P0A825
-
-
-
r
L-serine + tetrahydrofolate
glycine + 5,10-methylenetetrahydrofolate + H2O
show the reaction diagram
-
-
-
r
L-serine + tetrahydrofolate
glycine + 5,10-methylenetetrahydrofolate + H2O
show the reaction diagram
-
-
-
-
L-serine + tetrahydrofolate
glycine + 5,10-methylenetetrahydrofolate + H2O
show the reaction diagram
-
-
-
-
L-serine + tetrahydrofolate
glycine + 5,10-methylenetetrahydrofolate + H2O
show the reaction diagram
-
-
-
-
?
L-serine + tetrahydrofolate
glycine + 5,10-methylenetetrahydrofolate + H2O
show the reaction diagram
-
-
-
-
r
L-serine + tetrahydrofolate
glycine + 5,10-methylenetetrahydrofolate + H2O
show the reaction diagram
-
-
-
r
L-serine + tetrahydrofolate
glycine + 5,10-methylenetetrahydrofolate + H2O
show the reaction diagram
-
-
-
r
L-serine + tetrahydrofolate
glycine + 5,10-methylenetetrahydrofolate + H2O
show the reaction diagram
-
-
-
-
-
L-serine + tetrahydrofolate
glycine + 5,10-methylenetetrahydrofolate + H2O
show the reaction diagram
-
-
-
-
r
L-serine + tetrahydrofolate
glycine + 5,10-methylenetetrahydrofolate + H2O
show the reaction diagram
-
-
-
-
L-serine + tetrahydrofolate
glycine + 5,10-methylenetetrahydrofolate + H2O
show the reaction diagram
-
-
-
-
L-serine + tetrahydrofolate
glycine + 5,10-methylenetetrahydrofolate + H2O
show the reaction diagram
-
-
-
-
?
L-serine + tetrahydrofolate
glycine + 5,10-methylenetetrahydrofolate + H2O
show the reaction diagram
-
-
-
-
L-serine + tetrahydrofolate
glycine + 5,10-methylenetetrahydrofolate + H2O
show the reaction diagram
-
-
-
-
?
L-serine + tetrahydrofolate
glycine + 5,10-methylenetetrahydrofolate + H2O
show the reaction diagram
-
-
-
-
L-serine + tetrahydrofolate
glycine + 5,10-methylenetetrahydrofolate + H2O
show the reaction diagram
-
-
-
-
L-serine + tetrahydrofolate
glycine + 5,10-methylenetetrahydrofolate + H2O
show the reaction diagram
-
-
-
-
-
L-serine + tetrahydrofolate
glycine + 5,10-methylenetetrahydrofolate + H2O
show the reaction diagram
-
-
-
-
L-serine + tetrahydrofolate
glycine + 5,10-methylenetetrahydrofolate + H2O
show the reaction diagram
-
-
-
-
?
L-serine + tetrahydrofolate
glycine + 5,10-methylenetetrahydrofolate + H2O
show the reaction diagram
-
-
-
r
L-serine + tetrahydrofolate
glycine + 5,10-methylenetetrahydrofolate + H2O
show the reaction diagram
-
-
-
r
L-serine + tetrahydrofolate
glycine + 5,10-methylenetetrahydrofolate + H2O
show the reaction diagram
-
-
-
-
r
L-serine + tetrahydrofolate
glycine + 5,10-methylenetetrahydrofolate + H2O
show the reaction diagram
-
-
-
r
L-serine + tetrahydrofolate
glycine + 5,10-methylenetetrahydrofolate + H2O
show the reaction diagram
-
-
-
r
L-serine + tetrahydrofolate
glycine + 5,10-methylenetetrahydrofolate + H2O
show the reaction diagram
-
-
-
r
L-serine + tetrahydrofolate
glycine + 5,10-methylenetetrahydrofolate + H2O
show the reaction diagram
-
-
-
-
r
L-serine + tetrahydrofolate
glycine + 5,10-methylenetetrahydrofolate + H2O
show the reaction diagram
-
-
-
r
L-serine + tetrahydrofolate
glycine + 5,10-methylenetetrahydrofolate + H2O
show the reaction diagram
-
-
-
-
L-serine + tetrahydrofolate
glycine + 5,10-methylenetetrahydrofolate + H2O
show the reaction diagram
-
-
-
r
L-serine + tetrahydrofolate
glycine + 5,10-methylenetetrahydrofolate + H2O
show the reaction diagram
-
-
-
-
L-serine + tetrahydrofolate
glycine + 5,10-methylenetetrahydrofolate + H2O
show the reaction diagram
-
-
-
-
L-serine + tetrahydrofolate
glycine + 5,10-methylenetetrahydrofolate + H2O
show the reaction diagram
Q7SIB6
-
-
-
?
L-serine + tetrahydrofolate
glycine + 5,10-methylenetetrahydrofolate + H2O
show the reaction diagram
-
-
-
-
?
L-serine + tetrahydrofolate
glycine + 5,10-methylenetetrahydrofolate + H2O
show the reaction diagram
-
-
-
r
L-serine + tetrahydrofolate
glycine + 5,10-methylenetetrahydrofolate + H2O
show the reaction diagram
-
-
-
-
L-serine + tetrahydrofolate
glycine + 5,10-methylenetetrahydrofolate + H2O
show the reaction diagram
-
-
-
-
L-serine + tetrahydrofolate
glycine + 5,10-methylenetetrahydrofolate + H2O
show the reaction diagram
-
-
-
-
-
L-serine + tetrahydrofolate
glycine + 5,10-methylenetetrahydrofolate + H2O
show the reaction diagram
-
-
-
-
L-serine + tetrahydrofolate
glycine + 5,10-methylenetetrahydrofolate + H2O
show the reaction diagram
-
-
-
-
L-serine + tetrahydrofolate
glycine + 5,10-methylenetetrahydrofolate + H2O
show the reaction diagram
-
-
-
-
L-serine + tetrahydrofolate
glycine + 5,10-methylenetetrahydrofolate + H2O
show the reaction diagram
-
-
-
-
L-serine + tetrahydrofolate
glycine + 5,10-methylenetetrahydrofolate + H2O
show the reaction diagram
-
-
-
r
L-serine + tetrahydrofolate
glycine + 5,10-methylenetetrahydrofolate + H2O
show the reaction diagram
-
-
-
-
r
L-serine + tetrahydrofolate
glycine + 5,10-methylenetetrahydrofolate + H2O
show the reaction diagram
-
-
-
r
L-serine + tetrahydrofolate
glycine + 5,10-methylenetetrahydrofolate + H2O
show the reaction diagram
-
-
-
-
?
L-serine + tetrahydrofolate
glycine + 5,10-methylenetetrahydrofolate + H2O
show the reaction diagram
-
-
-
-
L-serine + tetrahydrofolate
glycine + 5,10-methylenetetrahydrofolate + H2O
show the reaction diagram
-
-
-
-
?
L-serine + tetrahydrofolate
glycine + 5,10-methylenetetrahydrofolate + H2O
show the reaction diagram
-
-
-
r
L-serine + tetrahydrofolate
glycine + 5,10-methylenetetrahydrofolate + H2O
show the reaction diagram
-
-
-
r
L-serine + tetrahydrofolate
glycine + 5,10-methylenetetrahydrofolate + H2O
show the reaction diagram
-
-
-
-
?
L-serine + tetrahydrofolate
glycine + 5,10-methylenetetrahydrofolate + H2O
show the reaction diagram
-
-
-
-
?
L-serine + tetrahydrofolate
glycine + 5,10-methylenetetrahydrofolate + H2O
show the reaction diagram
-
-
-
-
?
L-serine + tetrahydrofolate
glycine + 5,10-methylenetetrahydrofolate + H2O
show the reaction diagram
-
-
-
-
L-serine + tetrahydrofolate
glycine + 5,10-methylenetetrahydrofolate + H2O
show the reaction diagram
-
-
-
r
L-serine + tetrahydrofolate
glycine + 5,10-methylenetetrahydrofolate + H2O
show the reaction diagram
-
-
-
-
?
L-serine + tetrahydrofolate
glycine + 5,10-methylenetetrahydrofolate + H2O
show the reaction diagram
-
-
-
r
L-serine + tetrahydrofolate
glycine + 5,10-methylenetetrahydrofolate + H2O
show the reaction diagram
-
-
-
r
L-serine + tetrahydrofolate
glycine + 5,10-methylenetetrahydrofolate + H2O
show the reaction diagram
-
-
-
-
?
L-serine + tetrahydrofolate
glycine + 5,10-methylenetetrahydrofolate + H2O
show the reaction diagram
-
-
-
-
-
L-serine + tetrahydrofolate
glycine + 5,10-methylenetetrahydrofolate + H2O
show the reaction diagram
-
-
-
-
r
L-serine + tetrahydrofolate
glycine + 5,10-methylenetetrahydrofolate + H2O
show the reaction diagram
Q86LS9
-
-
-
?
L-serine + tetrahydrofolate
glycine + 5,10-methylenetetrahydrofolate + H2O
show the reaction diagram
Q2TL58
-
-
-
?
L-serine + tetrahydrofolate
glycine + 5,10-methylenetetrahydrofolate + H2O
show the reaction diagram
-
regulatory protein
-
-
L-serine + tetrahydrofolate
glycine + 5,10-methylenetetrahydrofolate + H2O
show the reaction diagram
-
regulatory protein
-
-
L-serine + tetrahydrofolate
glycine + 5,10-methylenetetrahydrofolate + H2O
show the reaction diagram
-
major pathway for production of C1-units of 5,10-methylenetetrahydrofolate
-
-
L-serine + tetrahydrofolate
glycine + 5,10-methylenetetrahydrofolate + H2O
show the reaction diagram
-
major pathway for production of C1-units of 5,10-methylenetetrahydrofolate
-
-
L-serine + tetrahydrofolate
glycine + 5,10-methylenetetrahydrofolate + H2O
show the reaction diagram
-
major pathway for production of C1-units of 5,10-methylenetetrahydrofolate
-
-
L-serine + tetrahydrofolate
glycine + 5,10-methylenetetrahydrofolate + H2O
show the reaction diagram
-
major pathway for production of C1-units of 5,10-methylenetetrahydrofolate
-
-
L-serine + tetrahydrofolate
glycine + 5,10-methylenetetrahydrofolate + H2O
show the reaction diagram
-
major pathway for production of C1-units of 5,10-methylenetetrahydrofolate
-
-
L-serine + tetrahydrofolate
glycine + 5,10-methylenetetrahydrofolate + H2O
show the reaction diagram
-
enzyme is a component of thymidylate cycle
-
-
L-serine + tetrahydrofolate
glycine + 5,10-methylenetetrahydrofolate + H2O
show the reaction diagram
-
enzyme is a component of thymidylate cycle
-
-
L-serine + tetrahydrofolate
glycine + 5,10-methylenetetrahydrofolate + H2O
show the reaction diagram
-
may play important role in central nervous system
-
-
L-serine + tetrahydrofolate
glycine + 5,10-methylenetetrahydrofolate + H2O
show the reaction diagram
-
main glycine source for purine biosynthetic pathway in ureide biogenesis
-
-
L-serine + tetrahydrofolate
glycine + 5,10-methylenetetrahydrofolate + H2O
show the reaction diagram
-
main glycine source for purine biosynthetic pathway in ureide biogenesis
-
-
L-serine + tetrahydrofolate
glycine + 5,10-methylenetetrahydrofolate + H2O
show the reaction diagram
-
main glycine source for purine biosynthetic pathway in ureide biogenesis
-
-
L-serine + tetrahydrofolate
glycine + 5,10-methylenetetrahydrofolate + H2O
show the reaction diagram
-
key enzyme of serine pathway for assimilation of C1-compounds
-
-
L-serine + tetrahydrofolate
glycine + 5,10-methylenetetrahydrofolate + H2O
show the reaction diagram
-
key enzyme of serine pathway for assimilation of C1-compounds
-
-
L-serine + tetrahydrofolate
glycine + 5,10-methylenetetrahydrofolate + H2O
show the reaction diagram
-
key enzyme of serine pathway for assimilation of C1-compounds
-
-
L-serine + tetrahydrofolate
glycine + 5,10-methylenetetrahydrofolate + H2O
show the reaction diagram
-
key enzyme of serine pathway for assimilation of C1-compounds
-
-
L-serine + tetrahydrofolate
glycine + 5,10-methylenetetrahydrofolate + H2O
show the reaction diagram
-
key enzyme of serine pathway for assimilation of C1-compounds
-
-
L-serine + tetrahydrofolate
glycine + 5,10-methylenetetrahydrofolate + H2O
show the reaction diagram
-
key enzyme of serine pathway for assimilation of C1-compounds
-
-
L-serine + tetrahydrofolate
glycine + 5,10-methylenetetrahydrofolate + H2O
show the reaction diagram
-
catalyzes interconversion of serine and glycine
-
-
L-serine + tetrahydrofolate
glycine + 5,10-methylenetetrahydrofolate + H2O
show the reaction diagram
-
catalyzes interconversion of serine and glycine
-
-
L-serine + tetrahydrofolate
glycine + 5,10-methylenetetrahydrofolate + H2O
show the reaction diagram
-
catalyzes interconversion of serine and glycine
-
-
L-serine + tetrahydrofolate
glycine + 5,10-methylenetetrahydrofolate + H2O
show the reaction diagram
-
enzyme plays a pivotal role in channelling metabolites between amino acid and nucleotide metabolism
-
-
L-serine + tetrahydrofolate
glycine + 5,10-methylenetetrahydrofolate + H2O
show the reaction diagram
-
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
show the reaction diagram
-
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
show the reaction diagram
-
L-serine is the physiological substrate
-
-
?
L-serine + tetrahydrofolate
glycine + 5,10-methylenetetrahydrofolate + H2O
show the reaction diagram
-
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
show the reaction diagram
Leishmania donovani MHOM/IN/80/Dd8
Q86LS9
-
-
-
?
L-serine + tetrahydrofolate
glycine + 5,10-methylenetetrahydrofolate + H2O
show the reaction diagram
Euglena gracilis Z
-
-
-
r
L-serine + tetrahydrofolate
glycine + 5,10-methylenetetrahydrofolate + H2O
show the reaction diagram
Euglena gracilis Z
-
-
-
-
L-serine + tetrahydrofolate
glycine + 5,10-methylenetetrahydrofolate + H2O
show the reaction diagram
Saccharomyces cerevisiae 3701B
-
-
-
-
?
L-serine + tetrahydrofolate
glycine + 5,10-methylenetetrahydrofolate + H2O
show the reaction diagram
Saccharomyces cerevisiae 3701B
-
key enzyme of serine pathway for assimilation of C1-compounds
-
-
L-serine + tetrahydrofolate
glycine + 5,10-methylenetetrahydrofolate + H2O
show the reaction diagram
Plasmodium falciparum strainTM4
-
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
show the reaction diagram
-
key enzyme of serine pathway for assimilation of C1-compounds
-
-
L-serine + tetrahydrofolate
glycine + 5,10-methylenetetrahydrofolate + H2O
show the reaction diagram
Danio rerio AB
Q2TL58
-
-
-
?
L-serine + tetrahydrofolate
glycine + 5,10-methylenetetrahydrofolate + H2O
show the reaction diagram
Corynebacterium glutamicum ATCC13032
-
-
-
-
?
L-serine + tetrahydrofolate
glycine + 5,10-methylenetetrahydrofolate + H2O
show the reaction diagram
Glycine max L.
-
-
-
r
L-serine + tetrahydrofolate
glycine + 5,10-methylenetetrahydrofolate + H2O
show the reaction diagram
Glycine max L.
-
main glycine source for purine biosynthetic pathway in ureide biogenesis
-
-
NADH + coenzyme Q10
?
show the reaction diagram
Q58992
-
-
-
?
tetrahydrofolate + L-Ser
5,10-methylenetetrahydrofolate + glycine
show the reaction diagram
P9WGI7, P9WGI9
-
-
-
r
tetrahydrofolate + L-Ser
5,10-methylenetetrahydrofolate + glycine
show the reaction diagram
P9WGI7, P9WGI9
-
-
-
r
tetrahydrofolate + L-Ser
? + glycine + H2O
show the reaction diagram
-
-
-
-
-
tetrahydrofolate + L-serine
5,10-methylenetetrahydrofolate + glycine + H2O
show the reaction diagram
Methanosaeta concilii, Methanospirillum hungatei, Methanolobus tindarius, Methanosarcina barkeri, Methanospirillum hungatei GP1, Methanosarcina barkeri DSM 804
-
-
-
-
?
tetrahydromethanopterin + L-Ser
glycine + ?
show the reaction diagram
-
-
-
-
?
tetrahydropteroylglutamate + L-Ser
glycine + ?
show the reaction diagram
-
-
-
-
?
L-serine + tetrahydropteroylglutamate
glycine + 5,10-methylene-tetrahydropteroylglutamate + H2O
show the reaction diagram
-
-
-
-
r
additional information
?
-
-
-
-
-
-
additional information
?
-
-
-
-
-
-
additional information
?
-
-
-
-
-
-
additional information
?
-
-
no: L-threonine
-
-
-
additional information
?
-
-
no: L-threonine
-
-
-
additional information
?
-
-
no: L-threonine
-
-
-
additional information
?
-
-
insoluble enzyme/antibody-complex shows 90% of original activity
-
-
-
additional information
?
-
-
no: D-serine
-
-
-
additional information
?
-
-
no: D-serine
-
-
-
additional information
?
-
-
no: D-serine
-
-
-
additional information
?
-
-
no: D-serine
-
-
-
additional information
?
-
-
no: D-serine
-
-
-
additional information
?
-
-
no: D-serine
-
-
-
additional information
?
-
P0A825
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
?
-
P0A825
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 transaminates D-alanine to pyruvate and pyridoxamine phosphate
-
-
-
additional information
?
-
-
enzyme transaminates D-alanine to pyruvate and pyridoxamine phosphate
-
-
-
additional information
?
-
P0A825
enzyme catalyses the racemization of D- and L-alanine
-
-
-
additional information
?
-
-
enzyme catalyses the racemization of D- and L-alanine
-
-
-
additional information
?
-
-
enzyme catalyses the racemization of D- and L-alanine
-
-
-
additional information
?
-
-
no: D-allothreonine
-
-
-
additional information
?
-
-
no: D-allothreonine
-
-
-
additional information
?
-
-
no: D-threonine
-
-
-
additional information
?
-
-
no: D-threonine
-
-
-
additional information
?
-
-
no: D-threonine
-
-
-
additional information
?
-
Q75BQ6
disruption of the SHM2 gene, encoding one of two serine hydroxymethyltransferase isoenzymes, reduces the flux from glycine to serine
-
-
-
additional information
?
-
-
low activity in placenta suggests that placental conversion of serine to glycine is not a major source of fetal glycine
-
-
-
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
?
-
-
the enzyme plays an indispensable role in nucleic acid biosynthesis
-
-
-
additional information
?
-
P9WGI7, P9WGI9
SHM1 does not undergo half-transamination reaction with D-Ala resulting in the formation of the apoenzyme
-
-
-
additional information
?
-
P9WGI7, P9WGI9
SHM2 does not undergo half-transamination reaction with D-Ala resulting in the formation of the apoenzyme
-
-
-
additional information
?
-
-
3-phenylserine is used as a substrate
-
-
-
additional information
?
-
-
human serine hydroxymethyltransferase 2 binds specifically to heterogeneous nuclear ribonucleoprotein D
-
-
-
additional information
?
-
Q7SIB6
SHMT also catalyses several tetrahydrofolate-independent side reactions such as cleavage of beta-hydroxy amino acids, transamination, racemization and decarboxylation
-
-
-
additional information
?
-
-
SHMT also catalyzes the tetrahydrofolate-independent retro-aldol cleavage of 3-hydroxy amino acids
-
-
-
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
?
-
-
broad substrate and reaction specificity, overview
-
-
-
additional information
?
-
I7H6W6
purified recombinant ApSHMT protein exhibits catalytic reactions for DL-threo-3-phenylserine as well as for L-serine
-
-
-
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
?
-
-
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 THF-independent aldolase activity, EC 4.1.2.5, toward beta-hydroxyamino acids, producing glycine and aldehydes
-
-
-
additional information
?
-
Q46A52
the enzyme also catalyzes the tetrahydrofolate-independent retroaldol cleavage of L-allo-threonine and L-threonine to glycine and acetaldehyde
-
-
-
additional information
?
-
Arabidopsis thaliana C24
-
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
?
-
Euglena gracilis Z
-
no: D-serine, no: D-allothreonine, no: D-threonine
-
-
-
additional information
?
-
Euglena gracilis Z
-
no: D-serine, no: D-allothreonine, no: D-threonine
-
-
-
additional information
?
-
Methanosarcina barkeri DSM 804
Q46A52
the enzyme also catalyzes the tetrahydrofolate-independent retroaldol cleavage of L-allo-threonine and L-threonine to glycine and acetaldehyde
-
-
-
additional information
?
-
Escherichia coli K-12 MG1655
-
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
?
-
-
the enzyme also exhibits tetrahydrofolate-independent aldolase activity, EC 4.1.2.5, toward beta-hydroxyamino acids, producing glycine and aldehydes
-
-
-
additional information
?
-
P9WGI7, P9WGI9
SHM2 does not undergo half-transamination reaction with D-Ala resulting in the formation of the apoenzyme
-
-
-
additional information
?
-
P9WGI7, P9WGI9
SHM1 does not undergo half-transamination reaction with D-Ala resulting in the formation of the apoenzyme
-
-
-
additional information
?
-
Rattus norvegicus Wistar
-
no: L-threonine, no: D-serine, enzyme catalyzes the pyridoxal 5'-phosphate dependent reversible cleavage of 3-hydroxy-alpha-amino acids, enzyme transaminates D-alanine to pyruvate and pyridoxamine phosphate, no: D-allothreonine
-
-
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
5,10-methylenetetrahydrofolate + glycine + H2O
tetrahydrofolate + L-Ser
show the reaction diagram
-
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
show the reaction diagram
-
-
-
-
?
5,10-methylenetetrahydrofolate + glycine + H2O
tetrahydrofolate + L-serine
show the reaction diagram
-
-
-
-
r
5,10-methylenetetrahydrofolate + glycine + H2O
tetrahydrofolate + L-serine
show the reaction diagram
-
-
-
-
?
5,10-methylenetetrahydrofolate + glycine + H2O
tetrahydrofolate + L-serine
show the reaction diagram
-
-
-
-
?
5,10-methylenetetrahydrofolate + glycine + H2O
tetrahydrofolate + L-serine
show the reaction diagram
I7H6W6
-
-
-
r
5,10-methylenetetrahydrofolate + glycine + H2O
tetrahydrofolate + L-serine
show the reaction diagram
Q94JQ3
-
-
-
r
5,10-methylenetetrahydrofolate + glycine + H2O
tetrahydrofolate + L-serine
show the reaction diagram
Hordeum vulgare Bob, Pisum sativum Progress 9
-
-
-
-
r
5,10-methylenetetrahydrofolate + glycine + H2O
tetrahydrofolate + L-serine
show the reaction diagram
-
-
-
-
?
L-Ser + tetrahydrofolate
Gly + 5,10-methylenetetrahydrofolate
show the reaction diagram
-
placental conversion of serine to glycine is a major source of fetal glycine
-
-
?
L-serine + tetrahydrofolate
glycine + 5,10-methylenetetrahydrofolate + H2O
show the reaction diagram
-
-
-
-
L-serine + tetrahydrofolate
glycine + 5,10-methylenetetrahydrofolate + H2O
show the reaction diagram
-
-
-
-
?
L-serine + tetrahydrofolate
glycine + 5,10-methylenetetrahydrofolate + H2O
show the reaction diagram
-
-
-
-
?
L-serine + tetrahydrofolate
glycine + 5,10-methylenetetrahydrofolate + H2O
show the reaction diagram
-
-
-
-
L-serine + tetrahydrofolate
glycine + 5,10-methylenetetrahydrofolate + H2O
show the reaction diagram
-
-
-
-
L-serine + tetrahydrofolate
glycine + 5,10-methylenetetrahydrofolate + H2O
show the reaction diagram
-
-
-
-
L-serine + tetrahydrofolate
glycine + 5,10-methylenetetrahydrofolate + H2O
show the reaction diagram
-
-
-
-
L-serine + tetrahydrofolate
glycine + 5,10-methylenetetrahydrofolate + H2O
show the reaction diagram
-
-
-
-
L-serine + tetrahydrofolate
glycine + 5,10-methylenetetrahydrofolate + H2O
show the reaction diagram
-
-
-
-
L-serine + tetrahydrofolate
glycine + 5,10-methylenetetrahydrofolate + H2O
show the reaction diagram
-
-
-
-
L-serine + tetrahydrofolate
glycine + 5,10-methylenetetrahydrofolate + H2O
show the reaction diagram
-
-
-
-
L-serine + tetrahydrofolate
glycine + 5,10-methylenetetrahydrofolate + H2O
show the reaction diagram
-
regulatory protein
-
-
L-serine + tetrahydrofolate
glycine + 5,10-methylenetetrahydrofolate + H2O
show the reaction diagram
-
regulatory protein
-
-
L-serine + tetrahydrofolate
glycine + 5,10-methylenetetrahydrofolate + H2O
show the reaction diagram
-
major pathway for production of C1-units of 5,10-methylenetetrahydrofolate
-
-
L-serine + tetrahydrofolate
glycine + 5,10-methylenetetrahydrofolate + H2O
show the reaction diagram
-
major pathway for production of C1-units of 5,10-methylenetetrahydrofolate
-
-
L-serine + tetrahydrofolate
glycine + 5,10-methylenetetrahydrofolate + H2O
show the reaction diagram
-
major pathway for production of C1-units of 5,10-methylenetetrahydrofolate
-
-
L-serine + tetrahydrofolate
glycine + 5,10-methylenetetrahydrofolate + H2O
show the reaction diagram
-
major pathway for production of C1-units of 5,10-methylenetetrahydrofolate
-
-
L-serine + tetrahydrofolate
glycine + 5,10-methylenetetrahydrofolate + H2O
show the reaction diagram
-
major pathway for production of C1-units of 5,10-methylenetetrahydrofolate
-
-
L-serine + tetrahydrofolate
glycine + 5,10-methylenetetrahydrofolate + H2O
show the reaction diagram
-
enzyme is a component of thymidylate cycle
-
-
L-serine + tetrahydrofolate
glycine + 5,10-methylenetetrahydrofolate + H2O
show the reaction diagram
-
enzyme is a component of thymidylate cycle
-
-
L-serine + tetrahydrofolate
glycine + 5,10-methylenetetrahydrofolate + H2O
show the reaction diagram
-
may play important role in central nervous system
-
-
L-serine + tetrahydrofolate
glycine + 5,10-methylenetetrahydrofolate + H2O
show the reaction diagram
-
main glycine source for purine biosynthetic pathway in ureide biogenesis
-
-
L-serine + tetrahydrofolate
glycine + 5,10-methylenetetrahydrofolate + H2O
show the reaction diagram
-
main glycine source for purine biosynthetic pathway in ureide biogenesis
-
-
L-serine + tetrahydrofolate
glycine + 5,10-methylenetetrahydrofolate + H2O
show the reaction diagram
-
main glycine source for purine biosynthetic pathway in ureide biogenesis
-
-
L-serine + tetrahydrofolate
glycine + 5,10-methylenetetrahydrofolate + H2O
show the reaction diagram
-
key enzyme of serine pathway for assimilation of C1-compounds
-
-
L-serine + tetrahydrofolate
glycine + 5,10-methylenetetrahydrofolate + H2O
show the reaction diagram
-
key enzyme of serine pathway for assimilation of C1-compounds
-
-
L-serine + tetrahydrofolate
glycine + 5,10-methylenetetrahydrofolate + H2O
show the reaction diagram
-
key enzyme of serine pathway for assimilation of C1-compounds
-
-
L-serine + tetrahydrofolate
glycine + 5,10-methylenetetrahydrofolate + H2O
show the reaction diagram
-
key enzyme of serine pathway for assimilation of C1-compounds
-
-
L-serine + tetrahydrofolate
glycine + 5,10-methylenetetrahydrofolate + H2O
show the reaction diagram
-
key enzyme of serine pathway for assimilation of C1-compounds
-
-
L-serine + tetrahydrofolate
glycine + 5,10-methylenetetrahydrofolate + H2O
show the reaction diagram
-
key enzyme of serine pathway for assimilation of C1-compounds
-
-
L-serine + tetrahydrofolate
glycine + 5,10-methylenetetrahydrofolate + H2O
show the reaction diagram
-
catalyzes interconversion of serine and glycine
-
-
L-serine + tetrahydrofolate
glycine + 5,10-methylenetetrahydrofolate + H2O
show the reaction diagram
-
catalyzes interconversion of serine and glycine
-
-
L-serine + tetrahydrofolate
glycine + 5,10-methylenetetrahydrofolate + H2O
show the reaction diagram
-
catalyzes interconversion of serine and glycine
-
-
L-serine + tetrahydrofolate
glycine + 5,10-methylenetetrahydrofolate + H2O
show the reaction diagram
-
enzyme plays a pivotal role in channelling metabolites between amino acid and nucleotide metabolism
-
-
L-serine + tetrahydrofolate
glycine + 5,10-methylenetetrahydrofolate + H2O
show the reaction diagram
Saccharomyces cerevisiae 3701B
-
key enzyme of serine pathway for assimilation of C1-compounds
-
-
L-serine + tetrahydrofolate
glycine + 5,10-methylenetetrahydrofolate + H2O
show the reaction diagram
-
key enzyme of serine pathway for assimilation of C1-compounds
-
-
L-serine + tetrahydrofolate
glycine + 5,10-methylenetetrahydrofolate + H2O
show the reaction diagram
Glycine max L.
-
main glycine source for purine biosynthetic pathway in ureide biogenesis
-
-
L-serine + tetrahydropteroylglutamate
glycine + 5,10-methylene-tetrahydropteroylglutamate + H2O
show the reaction diagram
-
-
-
-
r
additional information
?
-
Q75BQ6
disruption of the SHM2 gene, encoding one of two serine hydroxymethyltransferase isoenzymes, reduces the flux from glycine to serine
-
-
-
additional information
?
-
-
low activity in placenta suggests that placental conversion of serine to glycine is not a major source of fetal glycine
-
-
-
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
?
-
-
the enzyme plays an indispensable role in nucleic acid biosynthesis
-
-
-
additional information
?
-
-
SHMT also catalyzes the hydrolysis of 5,10-methenyl-tetrahydropteroylglutamate to 5-formyl-tetrahydropteroylglutamate
-
-
-
additional information
?
-
Arabidopsis thaliana C24
-
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
pyridoxal 5'-phosphate
-
requirement, 4 mol per mol enzyme
pyridoxal 5'-phosphate
-
requirement, 4 mol per mol enzyme
pyridoxal 5'-phosphate
-
requirement, 4 mol per mol enzyme
pyridoxal 5'-phosphate
-
not essential
pyridoxal 5'-phosphate
-
2 mol per mol enzyme
pyridoxal 5'-phosphate
-
-
pyridoxal 5'-phosphate
-
mechanism, active-site structure; requirement, 4 mol per mol enzyme
pyridoxal 5'-phosphate
-
-
pyridoxal 5'-phosphate
-
-
pyridoxal 5'-phosphate
-
important role in maintaining the structural integrity of the enzyme by preventing the dissociation of the enzyme into subunits, in addition to its function in catalysis
pyridoxal 5'-phosphate
-
important role in maintaining the structural integrity of the enzyme by preventing the dissociation of the enzyme into subunits, in addition to its function in catalysis; one mol/subunit bound to the epsilon-amino group of lysine
pyridoxal 5'-phosphate
-
important role in maintaining the structural integrity of the enzyme by preventing the dissociation of the enzyme into subunits, in addition to its function in catalysis; one mol per subunit
pyridoxal 5'-phosphate
-
-
pyridoxal 5'-phosphate
-
-
pyridoxal 5'-phosphate
-
-
pyridoxal 5'-phosphate
-
one mol/subunit bound to the epsilon-amino group of lysine
pyridoxal 5'-phosphate
-
2 mol per mol enzyme
pyridoxal 5'-phosphate
-
dimeric form of some mutant enzymes contains no pyridoxal 5'-phosphate
pyridoxal 5'-phosphate
-
mutant enzymes K226M and K226Q contain 1 mol of pyridoxal 5'-phosphate per mol of subunit. Pyridoxal 5'-phosphate is bound at the active site in an orientation different from that of the wild-type enzyme. K226 is responsible for flipping of pyridoxal 5'-phosphate from one orientation to another which is crucial for tetrahydropteroylglutamate-dependent Calpha-Cbeta bond cleavage of L-Ser
pyridoxal 5'-phosphate
P9WGI7, P9WGI9
SHM1 contains 1 mol per mol of enzyme dimer; SHM2 contains 2 mol per mol of enzyme dimer
pyridoxal 5'-phosphate
-
dependent on
pyridoxal 5'-phosphate
A9LDD9, Q7SXN1
;
pyridoxal 5'-phosphate
Q7SIB6
dependent on
pyridoxal 5'-phosphate
-
wild type enzyme contains 1 mol per mole of subunit
pyridoxal 5'-phosphate
-
the Kd for binding of the enzyme and pyridoxal 5'-phosphate is 0.00014 mM
pyridoxal 5'-phosphate
-
-
pyridoxal 5'-phosphate
-
-
pyridoxal 5'-phosphate
-
-
pyridoxal 5'-phosphate
-
-
pyridoxal 5'-phosphate
-
dependent on, the apo enzyme has some enzyme activity in the absence of pyridoxal 5'-phosphate but this activity is only slightly above background and can be due to incomplete removal of pyridoxal 5'-phosphate
pyridoxal 5'-phosphate
-
dependent on
pyridoxal 5'-phosphate
Q94JQ3
dependent on
pyridoxal 5'-phosphate
-
dependent on
pyridoxal 5'-phosphate
-
dependent on
pyridoxal 5'-phosphate
-
dependent on, stabilizes the dimeric form of the enzyme
pyridoxal 5'-phosphate
-
dependent on
pyridoxal 5'-phosphate
-
-
pyridoxal 5'-phosphate
I7H6W6
dependent on
pyridoxal 5'-phosphate
-
-
pyridoxal 5'-phosphate
-
stimulates activity
tetrahydrofolate
-
allosteric regulation; requirement with L-serine or L-2-methylserine as substrate
tetrahydrofolate
-
requirement with L-serine or L-2-methylserine as substrate
tetrahydrofolate
-
-
tetrahydrofolate
-
-
tetrahydrofolate
-
requirement with L-serine or L-2-methylserine as substrate
tetrahydrofolate
-
requirement with L-serine or L-2-methylserine as substrate
tetrahydrofolate
-
requirement with L-serine or L-2-methylserine as substrate
tetrahydrofolate
-
mechanism; requirement with L-serine or L-2-methylserine as substrate
tetrahydrofolate
-
requirement with L-serine or L-2-methylserine as substrate
tetrahydrofolate
-
requirement with L-serine or L-2-methylserine as substrate
tetrahydrofolate
-
-
tetrahydrofolate
-
requirement with L-serine or L-2-methylserine as substrate
Tetrahydrofolate derivatives
-
requirement, if L-serine is substrate
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Ca2+
-
activation at 0.5-10 mM
Mg2+
-
activation at 0.5-10 mM
Mn2+
-
activation at 0.5-10 mM
Zinc
-
within a mimosine-responsive transcriptional element localized within the first 50 base pairs of the human SHMT1 promoter, 50-base-pair sequence contains a consensus zinc-sensing metal regulatory element at position -44 to -38
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
1,10-phenanthroline
-
-
1,10-phenanthroline
-
-
2,2'-dipyridyl
-
-
2-aminoalanine
-
-
2-aminoisobutyrate
-
-
2-mercaptopropionic acid
-
-
4-chloro-L-threonine
-
-
4-chloro-L-threonine
-
-
4-chloro-L-threonine
-
-
4-chloro-L-threonine
-
-
4-chloro-L-threonine
-
-
5,10-methenyltetrahydrofolate
-
-
5,10-methylene-5,6,7,8-tetrahydrofolic acid
-
-
5,5-dithiobis(2-nitrobenzoic 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
-
-
allothreonine
-
-
aminoisobutyrate
-
-
aminopterin
-
-
aminopterin
-
-
Antibodies to cytosolic enzyme
-
-
-
Antibodies to mitochondrial enzyme
-
no inhibition of cytosolic enzyme
-
beta-Alanine
-
weak
beta-Alanine
-
-
beta-Aminoalanine
-
-
beta-chloroalanine
-
suicide substrate
Bromopyruvate
-
irreversible inactivation, substrates partially protect
Bromopyruvate
-
only cytoplasmac not mitochondrial enzyme
carboxymethoxylamine
-
strong
Chloroacetaldehyde
-
irreversible inactivation, substrates partially protect
Chloroacetaldehyde
-
only cytoplasmic not mitochondrial enzyme
Cibacron blue F3GA
-
complete inhibition, NAD(H) protects, reversible by tetrahydrofolate
Cibacron blue F3GA
-
reversible by dialysis
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
-
-
D-cycloserine
-
-
D-cycloserine
-
-
D-cycloserine
-
interaction extreme rapidly and irreversible
D-cycloserine
-
-
D-cycloserine
-
overexpression of SHMT-S increases resistance in a rich folate containing medium
Dichloromethotrexate
-
-
Dichloromethotrexate
-
-
dihydrofolate
-
-
DL-2-methylserine
-
-
DL-2-methylserine
-
-
DL-allothreonine
-
-
DL-O-Methylserine
-
-
Glycidaldehyde
-
directed to C1-binding-site
Glycidaldehyde
-
only cytoplasmic enzyme
glycine
-
-
glycine
-
-
glycine
-
-
glycine
-
glycine inhibits His6-tagged SHMT competitively with respect to serine and non-competitively with respect to tetrahydrofolate
guanidine hydrochloride
Q86LS9
86% loss of activity at 0.25 M
iodoacetamide
-
irreversible inactivation, substrates partially protect
iodoacetamide
-
only cytoplasmic not mitochondrial enzyme
L-alanine
-
-
L-alpha,beta-diaminopropionic acid
-
-
L-amino acids
-
weak, e.g. L-aspartic acid, ornithine, lysine, methionine, phenylalanine, homoserine, threonine, 4-aminobutyric acid
L-amino acids
-
-
L-cysteine
-
-
L-cysteine
-
mitochondrial enzyme
L-methionine
-
-
L-methionine
-
not
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
L-serine
-
competitive to glycine
L-serine
-
strong
L-serine
-
-
L-threonine
-
-
leucovorin
A9LDD9, Q7SXN1
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
methotrexate
-
-
methotrexate
-
-
methotrexate
-
-
methyl methanethiosulfonate
-
-
N-ethylmaleimide
-
-
NaCl
-
-
NaCl
I7H6W6
60% inhibition at 100 mM, restored to 66-71% activity in presence of 50 mM glycine betaine
NAD+
-
negative effector
O-phosphoserine
-
-
permetrexed
-
-
phenylhydrazine
-
partially reversible by pyridoxal 5'-phosphate
pyrimethamine
-
-
S-adenosyl-L-methionine
-
-
Sodium borohydride
-
-
tetrahydrofolate
Q86LS9
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
-
-
-
tetrahydropteroylglutamate
Q94JQ3
-
Thiosemicarbazide
-
poorly active against promastigotes, but SHMT-S transfectants can provide a small but significant resistance
Urea
Q86LS9
81% loss of activity at 1M
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
additional information
-
not: mercaptopropionic acid, mercaptoethanolamine; not: valine, leucine, glutamic acid, 3-hydroxybutyric acid
-
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
-
not: methionine, S-adenosyl-L-methionine, XMP, IMP, phosphoglycerate
-
additional information
-
not: ethanolamine, ethylenediamine; not: valine, leucine, glutamic acid, 3-hydroxybutyric acid
-
additional information
-
not: EDTA
-
additional information
-
not: iodoacetate
-
additional information
-
not: EDTA; not: purine nucleoside mono-, di- and triphosphates
-
additional information
-
inhibition kinetics
-
additional information
-
-
-
additional information
-
inhibition kinetics
-
additional information
-
not: N-/O-chloroacetyl and N-/O-bromoacetyl derivatives of glycine and L-serine
-
additional information
-
not: valine, leucine, glutamic acid, 3-hydroxybutyric acid
-
additional information
P34896
prototypes with negative total charge have greater affinity for Plasmodium falciparum SHMT than for human SHMT
-
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
Q94JQ3
model of uncompetitive substrate inhibition using tetrahydropteroylglutamates with different numbers of glutamate residues, overview
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
5,6,7,8-tetrahydrofolate
-
control of SHMT activity by the availability of 5,6,7,8-tetrahydrofolate
pyridoxal 5'-phosphate
-
-
pyridoxal 5'-phosphate
-
-
pyridoxal phosphate
-
-
L-serine
-
stabilizes the dimeric form of the enzyme
additional information
-
in the presence of 1mM dithiothreitol + 1mM pyridoxal 5-phosphate + 20 mM EDTA: 29fold increase in the specific activity
-
additional information
Q2TL58
higher concentrations of IPTG, increased induction temperature and/or prolonged induction time increase the ratio of insoluble and soluble SHMT-1
-
additional information
-
recombinant dominant negative SHMT1, DN2-SHMT1, localizes with lamin B1 and enhances SHMT1 activity for de novo thymidylate biosynthesis
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.002
(6S)-tetrahydrofolate
-
pH 7.2, 37C
0.071
D-serine
-
apparent value, in 50 mM HEPES, pH 8.0 containing 0.5 mM EDTA, 1 mM dithiothreitol, at 25C
47
D-serine
-
apparent value, in 50 mM HEPES buffer (pH 7.0), at 25C
0.68
glycine
-
pH 7.5, 70C
0.13
L-Ser
-
mutant enzyme P218A; mutant enzyme P218G
0.14
L-Ser
-
mutant enzyme P214A
0.24
L-Ser
-
mutant enzyme P214G
0.25
L-Ser
-
mutant enzyme P216A
0.3
L-Ser
-
wild-type enzyme
0.33
L-Ser
-
mutant enzyme P264A
0.58
L-Ser
-
mutant enzyme P216G
0.8
L-Ser
-
recombinant wild-type enzyme
0.8
L-Ser
-
pH 7.4, 37C
1
L-Ser
-
pH 7.4, 37C, wild-type enzyme
1.3
L-Ser
-
pH 7.4, 37C, mutant enzyme S52A
1.33
L-Ser
-
mutant enzyme P264G
4
L-Ser
-
mutant enzyme E75Q
5.2
L-Ser
-
pH 7.4, 37C, mutant enzyme R262A
8
L-Ser
-
mutant enzyme P258A
11.2
L-Ser
-
pH 7.4, 37C, mutant enzyme S52C
0.14
L-serine
-
apparent value, wild type enzyme, at 20C in 50 mM Na-HEPES (pH 7.2), containing 0.2 mM dithiothreitol and 0.1 mM EDTA
0.15 - 0.9
L-serine
-
-
0.15 - 0.9
L-serine
-
-
0.15 - 0.9
L-serine
-
-
0.15 - 0.9
L-serine
-
-
0.15 - 0.9
L-serine
-
-
0.15 - 0.9
L-serine
-
-
0.15 - 0.9
L-serine
-
recombinant enzyme
0.15 - 0.9
L-serine
-
recombinant enzyme
0.15 - 0.9
L-serine
-
mutant enzyme Y82F
0.15 - 0.9
L-serine
-
-
0.15
L-serine
-
apparent value, mutant enzyme L85A, at 20C in 50 mM Na-HEPES (pH 7.2), containing 0.2 mM dithiothreitol and 0.1 mM EDTA
0.18
L-serine
-
in 50 mM HEPES buffer (pH 7.0), at 25C
0.2
L-serine
-
apparent value, mutant enzyme L276A, at 20C in 50 mM Na-HEPES (pH 7.2), containing 0.2 mM dithiothreitol and 0.1 mM EDTA; apparent value, mutant enzyme L85A/L276A, at 20C in 50 mM Na-HEPES (pH 7.2), containing 0.2 mM dithiothreitol and 0.1 mM EDTA
0.2
L-serine
-
pH 7.2, 37C
0.22
L-serine
Q2TL58
-
0.251
L-serine
-
in phosphate buffer, pH 7.45, at 25C
0.28
L-serine
-
pH 7.5, 70C
0.29
L-serine
-
pH and temperature not specified in the publication
0.3
L-serine
-
wild-type enzyme, pH and temperature not specified in the publication
0.31
L-serine
-
pH and temperature not specified in the publication
0.371
L-serine
-
in 50 mM HEPES buffer, pH 7.45, at 25C
0.7
L-serine
-
only tetrameric form
0.7
L-serine
-
in 50 mM Tris-HCl pH 8.0, at 37C
0.9
L-serine
-
only dimeric form
0.9
L-serine
Q7SIB6
wild type enzyme, at 37C
1
L-serine
-
mitochondrial enzyme
1
L-serine
-
recombinant enzyme
1
L-serine
-
-
1
L-serine
Q7SIB6
mutant enzyme F315G, at 37C
1.3
L-serine
-
cytosolic enzyme
1.4
L-serine
-
-
1.5
L-serine
-
-
1.5
L-serine
-
mutant enzyme E74Q
1.6
L-serine
Q86LS9
-
1.8
L-serine
-
-
4
L-serine
-
mutant enzyme
25
L-serine
-
-
0.43
serine
A9LDD9, Q7SXN1
-
1.6
serine
Q86LS9
-
0.0037
tetrahydrofolate
-
mutant L474F
0.0041
tetrahydrofolate
-
wild-type
0.00435
tetrahydrofolate
-
apparent value, mutant enzyme L276A, at 20C in 50 mM Na-HEPES (pH 7.2), containing 0.2 mM dithiothreitol and 0.1 mM EDTA
0.00703
tetrahydrofolate
-
apparent value, wild type enzyme, at 20C in 50 mM Na-HEPES (pH 7.2), containing 0.2 mM dithiothreitol and 0.1 mM EDTA
0.00716
tetrahydrofolate
-
apparent value, mutant enzyme L85A, at 20C in 50 mM Na-HEPES (pH 7.2), containing 0.2 mM dithiothreitol and 0.1 mM EDTA
0.009
tetrahydrofolate
-
mutant L474F
0.01
tetrahydrofolate
-
mutant S394N
0.01
tetrahydrofolate
-
wild-type
0.0112
tetrahydrofolate
-
apparent value, mutant enzyme L85A/L276A, at 20C in 50 mM Na-HEPES (pH 7.2), containing 0.2 mM dithiothreitol and 0.1 mM EDTA
0.015
tetrahydrofolate
-
wild-type enzyme
0.017
tetrahydrofolate
-
mutant enzyme P218G; mutant enzyme P264A
0.019
tetrahydrofolate
-
mutant enzyme P218A
0.02
tetrahydrofolate
-
recombinant enzyme
0.02
tetrahydrofolate
-
mutant enzyme P214A; mutant enzyme P214G; mutant enzyme P216A
0.025
tetrahydrofolate
-
mutant S394N
0.04 - 0.046
tetrahydrofolate
-
-
0.04 - 0.046
tetrahydrofolate
-
glycine
0.04 - 0.046
tetrahydrofolate
-
recombinant enzyme
0.065
tetrahydrofolate
-
pH and temperature not specified in the publication
0.08
tetrahydrofolate
-
-
0.085
tetrahydrofolate
-
mutant enzyme P216G
0.086
tetrahydrofolate
-
pH and temperature not specified in the publication
0.14
tetrahydrofolate
-
in 50 mM HEPES buffer (pH 7.0), at 25C
0.193
tetrahydrofolate
-
in 50 mM HEPES buffer, pH 7.45, at 25C
0.2177
tetrahydrofolate
Q94JQ3
pH 8.5, temperature not specified in the publication, recombinant AtSHMT3
0.25
tetrahydrofolate
-
-
0.253
tetrahydrofolate
-
in phosphate buffer, at 25C
0.3
tetrahydrofolate
-
mutant K251R, without pyridoxal phosphate
0.82
tetrahydrofolate
-
recombinant enzyme
0.89
tetrahydrofolate
-
wild-type, in the presence of 0.25 mM pyridoxal phosphate
0.9
tetrahydrofolate
-
-
1
tetrahydrofolate
-
wild-type, without pyridoxal phosphate
1.16
tetrahydrofolate
-
mutant K251R, in the presence of 0.25 mM pyridoxal phosphate
2.1
tetrahydrofolate
-
mutant enzyme
2.4
tetrahydrofolate
Q86LS9
-
3.4
tetrahydrofolate
-
in 50 mM Tris-HCl pH 8.0, at 37C
0.1
tetrahydromethanopterin
-
pH 7.4, 37C
65.3
L-serine
-
-
additional information
additional information
-
allosteric kinetics
-
additional information
additional information
-
-
-
additional information
additional information
-
-
-
additional information
additional information
-
-
-
additional information
additional information
-
-
-
additional information
additional information
-
-
-
additional information
additional information
-
-
-
additional information
additional information
-
pH-dependence of kinetic parameters
-
additional information
additional information
-
-
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.246
D-serine
-
apparent value, in 50 mM HEPES, pH 8.0 containing 0.5 mM EDTA, 1 mM dithiothreitol, at 25C
0.26
D-serine
-
in 50 mM HEPES buffer (pH 7.0), at 25C
5
glycine
-
pH 7.5, 70C
0.02
L-Ser
-
mutant enzyme E75Q
0.12
L-Ser
-
mutant enzyme P264G
0.2
L-Ser
-
pH 7.4, 37C, mutant enzyme S52C
0.6
L-Ser
-
mutant enzyme P216G
0.7
L-Ser
-
pH 7.4, 37C, mutant enzyme S52A
0.8
L-Ser
-
pH 7.4, 37C, mutant enzyme R262A
1.6
L-Ser
-
mutant enzyme P264A
3.3
L-Ser
-
mutant enzyme P214A; mutant enzyme P214G; mutant enzyme P216A; mutant enzyme P218G
3.53
L-Ser
-
pH 7.4, 37C
4.2
L-Ser
-
pH 7.4, 37C, wild-type enzyme
4.5
L-Ser
-
mutant enzyme P218A
5
L-Ser
-
wild-type enzyme
10
L-Ser
-
recombinant wild-type enzyme
0.01
L-serine
-
mutant enzyme E74Q
0.0967
L-serine
-
mutant enzyme Y82F
0.16
L-serine
-
in 50 mM Tris-HCl pH 8.0, at 37C
0.43
L-serine
-
in phosphate buffer, pH 7.45, at 25C
0.7
L-serine
-
mutant enzyme
0.74
L-serine
-
in 50 mM HEPES buffer, pH 7.45, at 25C
0.98
L-serine
-
in 50 mM HEPES buffer (pH 7.0), at 25C
3.6
L-serine
-
only tetrameric form
3.9
L-serine
Q7SIB6
mutant enzyme F315G, at 37C; wild type enzyme, at 37C
4.1
L-serine
-
-
4.2
L-serine
-
-
5
L-serine
-
only dimeric form
5.85
L-serine
Q2TL58
-
6.7
L-serine
-
mutant enzyme L276A, at 20C in 50 mM Na-HEPES (pH 7.2), containing 0.2 mM dithiothreitol and 0.1 mM EDTA; mutant enzyme L85A/L276A, at 20C in 50 mM Na-HEPES (pH 7.2), containing 0.2 mM dithiothreitol and 0.1 mM EDTA
9.58
L-serine
-
-
10.5
L-serine
-
-
10.7
L-serine
-
-
10.8
L-serine
-
mutant enzyme L85A, at 20C in 50 mM Na-HEPES (pH 7.2), containing 0.2 mM dithiothreitol and 0.1 mM EDTA
11.4
L-serine
-
wild type enzyme, at 20C in 50 mM Na-HEPES (pH 7.2), containing 0.2 mM dithiothreitol and 0.1 mM EDTA
14.2
L-serine
-
recombinant enzyme
18.7
L-serine
-
pH 7.5, 70C
8.95
serine
A9LDD9, Q7SXN1
-
0.005
tetrahydrofolate
-
mutant K251R, without pyridoxal phosphate
0.02
tetrahydrofolate
-
mutant S394N, in the presence of pyridoxal phosphate
0.02167
tetrahydrofolate
-
mutant L474F, in the presence of pyridoxal phosphate
0.033
tetrahydrofolate
-
mutant L474F, in the presence of pyridoxal phosphate
0.04
tetrahydrofolate
-
wild-type, in the presence of pyridoxal phosphate
0.045
tetrahydrofolate
-
mutant S394N, in the presence of pyridoxal phosphate
0.07
tetrahydrofolate
-
wild-type, in the presence of pyridoxal phosphate
0.12
tetrahydrofolate
-
mutant enzyme P264G
0.6
tetrahydrofolate
-
mutant enzyme P216G
0.98
tetrahydrofolate
-
in 50 mM HEPES buffer (pH 7.0), at 25C
1.13
tetrahydrofolate
-
mutant K251R, in the presence of 0.25 mM pyridoxal phosphate
1.29
tetrahydrofolate
-
wild-type, without pyridoxal phosphate
1.3
tetrahydrofolate
-
wild-type, in the presence of 0.25 mM pyridoxal phosphate
1.6
tetrahydrofolate
-
mutant enzyme P264A
3.3
tetrahydrofolate
-
mutant enzyme P214A; mutant enzyme P214G; mutant enzyme P216A; mutant enzyme P218G
4.5
tetrahydrofolate
-
mutant enzyme P218A
5
tetrahydrofolate
-
wild-type enzyme
15.8
tetrahydrofolate
Q94JQ3
pH 8.5, temperature not specified in the publication, recombinant AtSHMT3
3.53
tetrahydromethanopterin
-
pH 7.4, 37C
640
L-serine
-
wild-type enzyme, pH and temperature not specified in the publication
additional information
additional information
-
-
-
additional information
additional information
-
-
-
additional information
additional information
-
-
-
additional information
additional information
-
-
-
additional information
additional information
-
-
-
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.00346
D-serine
-
apparent value, in 50 mM HEPES, pH 8.0 containing 0.5 mM EDTA, 1 mM dithiothreitol, at 25C
481
6.4
glycine
-
pH 7.5, 70C
72
1.99
L-serine
-
in 50 mM HEPES buffer, pH 7.45, at 25C
95
35.5
L-serine
-
wild-type enzyme, pH and temperature not specified in the publication
95
66.8
L-serine
-
pH 7.5, 70C
95
70
tetrahydrofolate
Q94JQ3
pH 8.5, temperature not specified in the publication, recombinant AtSHMT3
207
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
1.3
2-aminoalanine
-
-
3
5,10-methenyltetrahydrofolate
-
-
2.9
5,10-methylene-5,6,7,8-tetrahydrofolic acid
-
-
1.8
5-methyl-5,6,7,8-tetrahydrofolate
-
-
13 - 23
aminoisobutyrate
-
-
0.014
carboxymethoxylamine
-
-
40 - 55
D-alanine
-
-
2.02
D-cycloserine
-
-
3.9
DL-2-methylserine
-
soluble fraction
11.2
DL-2-methylserine
-
mitochondrial enzyme
2.7
DL-allothreonine
-
-
2.3
glycine
-
-
2.7 - 6.8
glycine
-
-
3
glycine
-
-
3
glycine
-
-
0.3
L-cysteine
-
-
0.7 - 0.9
L-serine
-
-
2.8
L-serine
-
-
0.085
tetrahydropteroylglutamate
Q94JQ3
pH 8.5, temperature not specified in the publication, recombinant AtSHMT3
50
L-threonine
-
-
additional information
additional information
-
comparison of Ki for allothreonine and threonine
-
additional information
additional information
-
-
-
additional information
additional information
-
-
-
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.15
1843U89
-
in 50 mM Tris-HCl pH 8.0, at 37C
0.15
AG331
-
in 50 mM Tris-HCl pH 8.0, at 37C
0.2
AG337
-
in 50 mM Tris-HCl pH 8.0, at 37C
0.5
D1694
-
IC50 above 0.5 mM, in 50 mM Tris-HCl pH 8.0, at 37C
0.15
GR1
-
in 50 mM Tris-HCl pH 8.0, at 37C
30
leucovorin
A9LDD9, Q7SXN1
-
70
leucovorin
A9LDD9, Q7SXN1
-
0.5
methotrexate
-
IC50 above 0.5 mM, in 50 mM Tris-HCl pH 8.0, at 37C
0.5
permetrexed
-
IC50 above 0.5 mM, in 50 mM Tris-HCl pH 8.0, at 37C
0.5
pyrimethamine
-
IC50 above 0.5 mM, in 50 mM Tris-HCl pH 8.0, at 37C
0.125
WR99210
-
in 50 mM Tris-HCl pH 8.0, at 37C
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.012
-
mutant enzyme E74Q
0.02
-
crude extract
0.0385
-
in the presence of glycine, in 200 mM HEPES buffer, pH 7.0
0.048
-
reaction of L-serine
0.05
-
mutant enzyme Y61A, using L-serine as substrate, at 37C
0.15
-
reaction of L-threonine
0.16
-
mutant enzyme Y82F
0.16
-
crude extract, in 50 mM HEPES (pH 7.0), 1 mM dithiothreitol and 0.5 mM EDTA at 25C
0.5
-
pH 7.2, 37C, extract from Escherichia coli cells carrying the expression vector
0.52
-
mutant enzyme
0.6
-
recombinant enzyme, crude extract
0.6
-
mutant enzyme
1.388
-
reaction of L-allothreonine
1.79
Q86LS9
-
1.86
-
after 3.8fold purification, in 50 mM HEPES (pH 7.0), 1 mM dithiothreitol and 0.5 mM EDTA at 25C
3.2
-
purified recombinant enzyme
4.1
-
only tetrameric form
4.2
-
-
4.3
-
-
4.3
-
pH 7.2, 37C, purified enzyme, recombinant
4.8
-
-
5
-
wild type enzyme, using L-serine as substrate, at 37C
5.46
Q2TL58
purified enzyme
6.7
-
only dimeric form
7.9
-
serine synthesis
10
-
recombinant enzyme
11.9
-
-
15.5
-
mitochondria
32.4
-
dimeric form at 80C
additional information
-
-
additional information
-
-
additional information
-
-
additional information
-
-
additional information
-
-
additional information
-
-
additional information
-
-
additional information
-
-
additional information
-
-
additional information
-
-
additional information
-
-
additional information
-
-
additional information
-
-
additional information
-
-
additional information
-
-
additional information
-
maximal activity of 6.3 U/mg total protein is reached
additional information
A5K8L9
isolated protein possesses functional activity as transformation into glycine auxotroph GS245 Escherichia coli shows that only pvshmt-transformed cells are able to complement the growth whereas the control cells require glycine supplementation
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7
A9LDD9, Q7SXN1
assay at; assay at
7.5 - 8
-
3-phenylserine degradation
7.8
-
mutant 3E7
8
-
serine synthesis
8
-
wild-type
8
-
in 50 mM HEPES
8.5
Q94JQ3
assay at
9
Q86LS9
enzyme retains more than 50% activity at pH 9.0
9
I7H6W6
assay at
additional information
-
pI, cytosolic enzyme: 4.5, pI, mitochondrial enzyme: 4.8
additional information
-
pI, cytosolic enzyme: 4.95, pI, mitochondrial enzyme: 5.3
additional information
-
pI: 4.2
additional information
-
-
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
4 - 10
-
activity range
6 - 8.5
-
cytosol: about 60% of maximal activity at pH 6, about 70% at 8.5, mitochondria: about 40% of maximal activity at pH 6.0 and 8.5
6 - 9
Q86LS9
-
6.5 - 10
-
-
6.5 - 9.5
-
about half-maximal activity at pH 6.5 and 9.5
7 - 9
-
serine synthesis: about 80% of maximal activity at pH 7.0 and 9.0
7.2 - 8.6
-
3-phenylserine degradation: about half-maximal activity at pH 7.2 and 8.6
7.3 - 9.5
-
about half-maximal activity at pH 7.3 and about 60% of maximal activity at 9.5
9.5
-
no activity above
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
25
I7H6W6
assay at
30
A9LDD9, Q7SXN1
assay at; assay at
35
-
2 optima: 35C and 55C
37 - 40
-
3-phenylserine degradation
37
-
serine synthesis
37
Q86LS9
assay at
55
-
2 optima: 35C and 55C
80
-
dimeric form of enzyme
80
-
retroaldol cleavage of L-allo-threonine
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5 - 30
-
the catalytic activity increases upon temperature increment
25 - 75
-
about half-maximal activity at 25C and 75C
28 - 37
Q2TL58
-
29 - 42
-
serine synthesis, about half-maximal activity at 28.5C and 90% of maximal activity at 42C
30 - 42
-
2-phenylserine degradation, about half-maximal activity at 29.5C and 80% of maximal activity at 42C
38 - 60
Q86LS9
-
additional information
-
thermograms of enzyme and mutant enzyme in the absence and presence of L-serine
additional information
Q86LS9
enzyme is thermally stable up to 45C where it exhibits 85% activity. At 65C it loses its activity
pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
preferentially expressed
Manually annotated by BRENDA team
Leishmania donovani MHOM/IN/80/Dd8
-
-
-
Manually annotated by BRENDA team
-
optimum growth temperature of 70-75C
Manually annotated by BRENDA team
-
optimum growth temperature of 70-75C
-
Manually annotated by BRENDA team
Danio rerio AB
-
-
-
Manually annotated by BRENDA team
A9LDD9, Q7SXN1
elevated mRNA expression detected by RT-PCT
Manually annotated by BRENDA team
-
transformed cells
Manually annotated by BRENDA team
-
SHMT activity of antisense lines is 70-90% lower than in the wild-type, negative effects of antisensed SHMT becomes increasingly severe with plant age
Manually annotated by BRENDA team
Hordeum vulgare Bob, Pisum sativum Progress 9
-
-
-
Manually annotated by BRENDA team
-
from rats fed dietary pyridoxine ranging from adequare to deficient levels, 2-0 mg pyridoxine per kg diet
Manually annotated by BRENDA team
A9LDD9, Q7SXN1
elevated mRNA expression detected by RT-PCT. Strong protein expression detected by western blotting
Manually annotated by BRENDA team
A9LDD9, Q7SXN1
siginificant protein expression detected by Western Blotting only in liver and ovary
Manually annotated by BRENDA team
-
inoculated with Rhizobium japonicum strain 311b142
Manually annotated by BRENDA team
Glycine max L.
-
inoculated with Rhizobium japonicum strain 311b142
-
Manually annotated by BRENDA team
A9LDD9, Q7SXN1
elevated mRNA expression detected by RT-PCT. Strong protein expression detected by western blotting
Manually annotated by BRENDA team
A9LDD9, Q7SXN1
siginificant protein expression detected by Western Blotting only in liver and ovary
Manually annotated by BRENDA team
-
activity per gram of placenta increases 2.1fold between midgestation and term
Manually annotated by BRENDA team
-
low activity, activity is similar 8 weeks post conception and at term
Manually annotated by BRENDA team
-
dominance of the SHM2 over SHM1 transcripts in roots
Manually annotated by BRENDA team
-
germinating
Manually annotated by BRENDA team
Q94JQ3
germinated, high expression level of AtSHMT3
Manually annotated by BRENDA team
-
early trophozoites lack visible organellar isozyme PfSHMTc, while it occurs during the mid-to-late trophozoite and schizont stages
Manually annotated by BRENDA team
-
protoxylem and/or adjacent cells, SHM1 and SHM2
Manually annotated by BRENDA team
-
both PfSHMTc and PfSHMTm are concentrated in the central region of the parasite that becomes the residual body on erythrocyte lysis and merozoite release
Manually annotated by BRENDA team
additional information
-
distribution
Manually annotated by BRENDA team
additional information
Q86LS9
gene is preferentially expressed in the amastigote stage of parasite
Manually annotated by BRENDA team
additional information
A9LDD9, Q7SXN1
RT-PCR results show that zmSHMT mRNA is evenly distributed among tissues. However zmSHMT protein expression does not correspond to the detected mRNA expression detected in most tissues
Manually annotated by BRENDA team
additional information
-
cellular distribution of SHM1 and SHM2, detailed overview
Manually annotated by BRENDA team
additional information
-
SHMT2alpha co-localizes with lamin B1 in SH-SY5Y cells. Recombinant dominant negative SHMT1, DN2-SHMT1, localizes with lamin B1 and enhances SHMT1 activity for de novo thymidylate biosynthesis
Manually annotated by BRENDA team
additional information
Leishmania donovani MHOM/IN/80/Dd8
-
gene is preferentially expressed in the amastigote stage of parasite
-
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
isozyme PfSHMTc in a stage-specific manner, isozyme PfSHMTc localization in this organelle is less restricted than for the mitochondrion and persists from the late trophozoite to the post-mitotic stages
Manually annotated by BRENDA team
Hordeum vulgare Bob, Pisum sativum Progress 9, Euglena gracilis Z
-
-
-
Manually annotated by BRENDA team
-
75% of the enzyme activity
Manually annotated by BRENDA team
-
isozyme PfSHMTc during all stages
Manually annotated by BRENDA team
-
SHMT1 encodes the cytoplasmic/nuclear isozyme SHMT1, SHMT2 encodes the mitochondrial isozyme SHMT2 and the cytoplasmic/nuclear isozyme SHMT2alpha through alternative promoter uses
Manually annotated by BRENDA team
Euglena gracilis Z, Rattus norvegicus Wistar
-
-
-
Manually annotated by BRENDA team
-
from rat liver fed dietary pyridoxine ranging from adequate to deficient levels, 2-0 mg pyridoxine per kg diet. SHMT activity increases with increasing dietary pyridoxine concentrations
Manually annotated by BRENDA team
A5K8L9
predicted to tbe cytosolic
Manually annotated by BRENDA team
A9LDD9, Q7SXN1
zcSHMT is detected in the cytosol as well as in the nucleus
Manually annotated by BRENDA team
Danio rerio AB
-
-
-
Manually annotated by BRENDA team
-
enzyme possesses a putative N-terminal hydrogenosomal presequence
Manually annotated by BRENDA team
-
3% of the enzyme activity
-
Manually annotated by BRENDA team
-
5% of the enzyme activity
Manually annotated by BRENDA team
-
from rat liver fed dietary pyridoxine ranging from adequate to deficient levels, 2-0 mg pyridoxine per kg diet. SHMT activity increases with increasing dietary pyridoxine concentrations. The mitochondrial isoenzyme comprises about 70% of the total activity
Manually annotated by BRENDA team
A9LDD9, Q7SXN1
peptide sequence alignment with the known SHMT from other species and the prospective zebrafish cytosolic SHMT as well as signal prediction software reveals a potential mitochondrial signal peptide cleavage site between residues 20 and 30
Manually annotated by BRENDA team
-
isozyme PfSHMTc in a stage-specific manner. Isozyme PfSHMTm showa a distinctly more pronounced mitochondrial location through most of the erythrocytic cycle, presence of a mitochondrial signal sequence
Manually annotated by BRENDA team
-
SHMT2 encodes the mitochondrial isozyme SHMT2 and the cytoplasmic/nuclear isozyme SHMT2alpha through alternative promoter uses
Manually annotated by BRENDA team
A9LDD9, Q7SXN1
zcSHMT is detected in the cytosol as well as in the nucleus
Manually annotated by BRENDA team
-
SHMT1 localizes to the nucleus in response to UV treatment
Manually annotated by BRENDA team
-
isozyme PfSHMTc during all stages
Manually annotated by BRENDA team
-
SHMT1 encodes the cytoplasmic/nuclear isozyme SHMT1, SHMT2 encodes the mitochondrial isozyme SHMT2 and the cytoplasmic/nuclear isozyme SHMT2alpha through alternative promoter uses. SHMT1, SHMT2alpha, thymidylate synthase, and dihydrofolate reductase are present in nuclei during S and G2/M phases
Manually annotated by BRENDA team
Euglena gracilis Z, Rattus norvegicus Wistar
-
-
-
Manually annotated by BRENDA team
additional information
-
isozymes in cytosol and mitochondria
-
Manually annotated by BRENDA team
additional information
-
isozymes in cytosol and mitochondria
-
Manually annotated by BRENDA team
additional information
-
comparison of cytosolic and mitochondrial forms of enzyme
-
Manually annotated by BRENDA team
additional information
-
comparison of cytosolic and mitochondrial forms of enzyme
-
Manually annotated by BRENDA team
additional information
-
immunochemically different
-
Manually annotated by BRENDA team
additional information
-
antigenically related
-
Manually annotated by BRENDA team
additional information
-
SHMT-L in an organelle that has hallmarks of the parasite mitochondrion
-
Manually annotated by BRENDA team
additional information
-
patterns of localization of the two isoforms during the parasite erythrocytic cycle, overview. Both PfSHMTc and PfSHMTm are concentrated in the central region of the parasite that becomes the residual body on erythrocyte lysis and merozoite release
-
Manually annotated by BRENDA team
additional information
Rattus norvegicus Wistar
-
isozymes in cytosol and mitochondria, antigenically related
-
-
Manually annotated by BRENDA team
PDB
SCOP
CATH
ORGANISM
Burkholderia cenocepacia (strain ATCC BAA-245 / DSM 16553 / LMG 16656 / NCTC 13227 / J2315 / CF5610)
Burkholderia cenocepacia (strain ATCC BAA-245 / DSM 16553 / LMG 16656 / NCTC 13227 / J2315 / CF5610)
Burkholderia cenocepacia (strain ATCC BAA-245 / DSM 16553 / LMG 16656 / NCTC 13227 / J2315 / CF5610)
Burkholderia cenocepacia (strain ATCC BAA-245 / DSM 16553 / LMG 16656 / NCTC 13227 / J2315 / CF5610)
Burkholderia pseudomallei (strain 1710b)
Campylobacter jejuni subsp. jejuni serotype O:2 (strain NCTC 11168)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Psychromonas ingrahamii (strain 37)
Rickettsia rickettsii (strain Sheila Smith)
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Staphylococcus aureus (strain COL)
Streptococcus thermophilus (strain CNRZ 1066)
Streptococcus thermophilus (strain CNRZ 1066)
Streptococcus thermophilus (strain CNRZ 1066)
Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
25000
-
refolded pyridoxal-5'-phosphate-binding domain of SHMT, gel filtration
704347
50000
-
sequence analysis
673412
50000
A9LDD9, Q7SXN1
SDS-PAGE; SDS-PAGE
686353
50600
-
sequence analysis, SHMT-S
675874
53100
-
sequence analysis, SHMT-L
675874
54000
Q86LS9
SDS-PAGE
676982
72400
-
gel filtration
703653
74000
-
gel filtration
719472
80000
-
HPLC gel filtration
441410
81500
-
calculated molecular weight
705603
85000
-
native enzyme, SDS-PAGE
705602
87100
P9WGI7, P9WGI9
SHM2, gel filtration
659265
88000
-
gel filtration
441437
90000
-
gel filtration
441409
90000
-
dimeric form; gel filtration
441432
91000
-
wild type SHMT exists as a dimer in both apo- and holo-forms, ultracentrifugation
703634
91000
-
SDS-PAGE
703674
91200
P9WGI7, P9WGI9
SHM1, gel filtration
659265
96000
-
sedimentation equilibrium centrifugation, amino acid composition
441412
98000
-
gel filtration
441410
98000
-
gel filtration
659269
100000 - 115000
-
HPLC gel filtration
441412
100000
-
gel filtration
726831
130000
-
apoenzyme, peak 2, gel filtration
441426
170000
-
mitochondria, sedimentation equilibrium centrifugation
441401
180000 - 200000
-
gel filtration, sucrose density gradient centrifugation
441413
180000 - 200000
-
-
676503
180000
-
tetrameric form, gel filtration
441432
185000
-
soluble, high speed sedimentation equilibrium centrifugation
441401
200000 - 204000
-
mitochondria, gel filtration, PAGE, amino acid composition
441399
200000
-
holoenzyme, apoenzyme: peak 1, gel filtration
441426
200000
Q2TL58
gel filtration, holo- and apoenzyme
676954
205000
-
gel filtration
441408
208000
-
gel filtration
441403
209000
-
gel filtration
441391
210000
-
gel filtration
441393
210000
-
wild-type and mutant enzyme, gelfiltation
441428
210000
-
gel filtration
657811, 658892
213000
-
gel filtration
441426
215000
-
gel filtration, amino acid composition
441394
215000
-
HPLC gel filtration
441405
216000
-
cytosol, PAGE
441399
216000
Q86LS9
gel filtration; gel filtration, tetramer
676982
220000
-
gel filtration
391984
220000
-
gel filtration
441398
220000
-
mutant enzyme
441430
230000
-
cytosol, amino acid composition, gel filtration
441399
230000
-
-
441407
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
?
-
x * 45000, SDS-PAGE
?
-
x * 49800, recombinant His-tagged PfSHMTc, SDS-PAGE
?
Escherichia coli AB90054
-
x * 45000, SDS-PAGE
-
dimer
-
2 * 45000, SDS-PAGE
dimer
-
2 * 44000, SDS-PAGE
dimer
-
2 * 53000, SDS-PAGE
dimer
-
2 * 48000, SDS-PAGE
dimer
-
2 * 46000, SDS-PAGE
dimer
-
gel filtration, crystallographic symmetry
dimer
-
removal of the bound pyridoxal 5'-phosphate from the mutant tetrameric enzyme leads to dissociation to a dimer
dimer
-
2 * 47000, calculated from DNA-sequence
dimer
Q7SIB6
x-ray crystallography
dimer
P9WGI7, P9WGI9
2 * 45000, SHM1, SDS-PAGE
dimer
P9WGI7, P9WGI9
2 * 45500, SHM2, SDS-PAGE
dimer
-
2 * 48200, SDS-PAGE
dimer
A5K8L9
predicted to be a dimer
dimer
-
in the 0.0025-0.025 mM subunit concentration range, the wild type SHMT is a dimer, either in the presence or absence of cofactor. The apo-L85A mutant enzyme is approximately 75% dimeric
dimer
-
native SHMT
dimer
-
homology modeling and comparison to SHMT from Bacillus stearothermophilus, using the crystal structure, PDB ID 1KKJ, overview
dimer
-
homology modeling using the crystal structure, PDB ID 1KKJ, and comparison to SHMT from Bacillus subtilis, overview
dimer
-
wild-type eSHMT is a dimer in both apo- and holo-enzyme forms
dimer
Euglena gracilis Z
-
2 * 45000, SDS-PAGE, 2 * 44000, SDS-PAGE
-
dimer
-
2 * 45500, SHM2, SDS-PAGE, 2 * 45000, SHM1, SDS-PAGE
-
dimer
-
2 * 53000, SDS-PAGE
-
homodimer
-
2 * 49000, SDS-PAGE
homodimer
-
2 * 43000, SDS-PAGE
homodimer
-
2 * 48700, SDS-PAGE
homodimer
-
immunoblotting
homodimer
-
2 * 55000, calculated from amino acid sequence
homodimer
-
2 * 55000, His-tagged enzyme, SDS-PAGE
homodimer
-
2 * 45047, calculated from sequence
homodimer
Methanosarcina barkeri DSM 804
-
2 * 43000, SDS-PAGE, 2 * 45047, calculated from sequence
-
homodimer
-
2 * 48700, SDS-PAGE
-
homodimer
Plasmodium falciparum strainTM4
-
2 * 55000, calculated from amino acid sequence
-
homotetramer
-
-
homotetramer
-
-
homotetramer
-
4 * 50000, SDS-PAGE
homotetramer
-
4 * 45000, SDS-PAGE
homotetramer
-
4 * 55000, SDS-PAGE
homotetramer
-
4 * 52000, SDS-PAGE
homotetramer
-
4 * 53000, SDS-PAGE
homotetramer
-
4 * 53000, SDS-PAGE
homotetramer
-
4 * 53000, SDS-PAGE
homotetramer
-
4 * 54000, SDS-PAGE
homotetramer
-
4 * 56000, SDS-PAGE
homotetramer
-
4 * 56300, cytosol, SDS-PAGE
homotetramer
-
4 * 53700, mitochondria, SDS-PAGE
homotetramer
-
4 * 53000, mutant enzyme
homotetramer
-
lithium(dodecyl sulfate)-PAGE
homotetramer
Rattus norvegicus Wistar
-
4 * 56300, cytosol, SDS-PAGE, 4 * 53700, mitochondria, SDS-PAGE
-
homotetramer
Glycine max L.
-
4 * 55000, SDS-PAGE
-
tetramer
-
4 * 53000, SDS-PAGE
tetramer
-
4 * 50000, gel filtration
tetramer
-
4 * 53000, wild-type enzyme and mutant enzymes C203F and W110F, SDS-PAGE
tetramer
-
4 * 50000, Western blot analysis
tetramer
Q86LS9
4 * 54000, SDS-PAGE, gel filtration
tetramer
Q2TL58
x * 53000, SDS-PAGE, x * 53317, sequence analysis
tetramer
Q86LS9
4 * 54000 Da, gel filtration
tetramer
Leishmania donovani MHOM/IN/80/Dd8
-
4 * 54000, SDS-PAGE, gel filtration, 4 * 54000 Da, gel filtration
-
tetramer
Danio rerio AB
-
x * 53000, SDS-PAGE, x * 53317, sequence analysis
-
monomer
-
the apo-L276A and the apo-L85A mutants are in the monomeric state
additional information
-
90% dimer and 10% tetramer in the same organism, one subunit: 45000 Da, SDS-PAGE
additional information
-
the folding mechanism of SHMT is divided in two phases and terminates with pyridoxal 5'-phosphate binding. In the first one, the large and small domains rapidly assume their native state, forming a folding intermediate that is not able to bind pyridoxal 5'-phosphate. In the second, slower phase, the enzyme folds into the native structure, acquiring the capability to bind the cofactor. Importance of the third hydrophobic cluster, highly conserved in type I fold enzyme, as key structural determinant of the assembly of eSHMT active site and overall native fold. This cluster plays a fundamental role in the transition from the first to the second phase of SHMT folding process
additional information
-
the folding mechanism of SHMT is divided in two phases and terminates with pyridoxal 5'-phosphate binding. In the first one, the large and small domains rapidly assume their native state, forming a folding intermediate that is not able to bind pyridoxal 5'-phosphate. In the second, slower phase, the enzyme folds into the native structure, acquiring the capability to bind the cofactor. Importance of the third hydrophobic cluster, highly conserved in typr I fold enzymes, as key structural determinant of the assembly of eSHMT active site and overall native fold. This cluster plays a fundamental role in the transition from the first to the second phase of SHMT folding process
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
side-chain modification
-
in addition to the lysine residue involved in Schiff base formation with the PLP, other residues like arginine, histidine, cysteine and tryptophan essential for catalysis, review
side-chain modification
-
in addition to the lysine residue involved in Schiff base formation with the PLP, other residues like arginine, histidine, cysteine and tryptophan essential for catalysis, review
additional information
-
enzyme is a mRNA binding protein
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
crystals of K226M and K226Q mutant enzymes and of the complex of mutant enzyme K226Q with Gly or mutant enzyme K226M with Ser. Crystals are obtained by mixing 0.004 ml of protein solution 0.375 mM with 0.004 mM of reservoir solution containing 100 mM Hepes buffer, pH 7.5, 0.2 mM EDTA, 5 mM 2-mercaptoethanol, and 50% 2-methyl-2,4-pentanediol
-
crystals of Y51F and Y61A SHMT mutants are obtained by hanging drop vapour diffusion using 50% (v/v) 2-methyl 2,4-pentanediol as the precipitant
-
internal aldimine form, external aldimine form with bound serine and glycine, ternary complex with glycine and 5-formyl tetrahydrofolate
-
mutant proteins are crystallized by the hanging drop vapor diffusion method, using 50% 2-methyl 2,4-pentanediol as the precipitant with 0.2 mM EDTA, 5 mM beta-mercaptoethanol in 100 mM HEPES (pH 7.5)
Q7SIB6
crystal structure of the apoenzyme and pyridoxal 5'-phosphate-bound holoenzyme at 2.83 and 3.0 A resolution, respectively. The crystal structure of archaeal serine hydroxymethyltransferase reveals idiosyncratic features likely required to withstand high temperatures
Q58992
crystal structure at 2.7 A resolution of the recombinant enzyme with active-site bound 5-formyl-tetrahydropteroylglutamate is obtained by soaking unliganded crystals of of the recombinant enzyme in 5-formyl-tetrahydropteroylglutamate, the conformation of the pteridine ring and its interactions with the enzyme differ slightly from those observed in complexes of the monoglutamate cofactor
-
hanging-drop vapour diffusion technique. Crystals of both mutants, E75L and E75Q are obtained by mixing 0.003v ml of an enzyme solution (34-44 mg/ml in 20 mM potassium phosphate, pH 7.3, with 1 mM dithiothreitol) with an equal volume of reservoir solution. The reservoir solution for E75L rcSHMT consists of 50 mM potassium phosphate, pH 6.6, 8.5-9.1% PEG 8000, and 100 mM KCl. For E75Q rcSHMT the reservoir solution consists of 15 mM potassium 2-(N-morpholino)ethanesulfonate, pH 6.4, 8.5-10% PEG 4000, and 30 mM KCl. Serine complexes are formed by adding 0.00025 ml of 250 mM L-serine directly to the drop
-
mitochondrial enzyme
-
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5.8 - 8.5
-
stable, rabbit cytosol
441420
6 - 7.5
-
stable
441410
6 - 8.5
-
stable
441412
7.2 - 8.3
-
stable, at pH 8.55: loss of activity, tetrameric holoenzyme dissociates into the dimeric form, at pH 9.3: complete dissociation
441426
8
P9WGI7, P9WGI9
transition of SHM2 is between pH 6.5 and 11 and centered at about pH 8.0
659265
9
P9WGI7, P9WGI9
native SHM2 dimer dissociates into monomer
659265
9.25
P9WGI7, P9WGI9
transition of SHM1 is between pH 8 and 11 and centered at about pH 9.25
659265
10.5
P9WGI7, P9WGI9
resistant to alkaline denaturation up to, SHM1
659265
additional information
-
recombinant wild-type bsSHMT and chimeric mutant enzyme are significantly higher susceptible to proteolysis into smaller protein fragments at pH 11 as compared to neutral pH
718968
additional information
-
recombinant wild-type bstSHMT and chimeric mutant enzyme are only merginally susceptible to proteolysis into smaller protein fragments at pH 11 and at neutral pH
718968
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
30 - 65
-
a broad sigmoidal transition between 30C and 65C having an apparent Tm of about 48C is observed for the native dimeric SHMT molecule, SHMT is a noncooperative molecule which starts losing the structure from very low temperature (30C) and loses most of ist secondary structure at relatively high temperature
704347
30
-
several h, pH 5.8-8.5, cytosol
441420
40
-
below, at least 10 min stable
441410
45
-
above, rapid loss of activity
441410
50
-
20 min stable
441403
52
-
apoenzyme, absence of pyridoxal 5'-phosphate
441426
55
-
t1/2: about 2 min, glycerol stabilizes
441413
55
-
Tm-value for wild-type enzyme and mutant enzymes R262A, S52C and S52A without ligands or with Gly as ligand. Tm-value for mutant enzymes mutant enzymes R262A, S52C and S52A with L-Ser as ligand
658892
58
-
holoenzyme
441426
60
-
subunit interactions retained
441393
60
-
enzyme stable in the absence of any ligand
441432
60
P9WGI7, P9WGI9
transition temperature of SHM1
659265
60
-
for 10 min, the native enzyme conserves about 40% of its activity, while the mutant 3E7 retains about 56% of its activity
673397
65
-
85% loss of activity after 20 min
441403
65
Q7SIB6
the melting temperature of the wild type enzyme is at 65C
702126
67
-
Tm-value for wild-type enzyme in absence of Ser
659237
68
-
Tm-value for wild-type enzyme with L-Ser as ligand
658892
69
P9WGI7, P9WGI9
transition temperature of SHM1
659265
70
-
complete loss of activity after 6 min, enzyme-antibody complex: 30% loss of activity after 20 min
441403
70
-
50% loss of activity in the absence of any ligand
441432
73
-
Tm-value for wild-type enzyme in presence of Ser
659237
additional information
-
enzyme-antibody complex more stable to elevated temperatures than free enzyme, allosteric effectors fail to protect free enzyme; L-serine protects against thermal inactivation
441403
additional information
-
glycerol, 30% v/v, enhances thermal stability
441413
additional information
-
L-serine increases the thermal stability; Tm of wild-type and mutant enzyme: 54C, in the presence of serine Tm of wild-type enzyme: 63C
441428
additional information
-
L-serine increases the thermal stability; Tm: 55C, increased to 65C in the presence of L-serine, Tm: 68C mutant enzyme Y82F in the presence of serine
441430
additional information
-
L-serine increases the thermal stability; pyridoxal 5'-phosphate increases the thermal stability; Tm values of enzyme and dimeric and tetrameric forms in the absence and presence of ligands
441432
additional information
-
thermal denaturation is irreversible
659237
additional information
-
thermophilic enzyme. Thermal stability of SHMT can be achieved mainly through three strategies: 1. increased number of charged residues at the protein surface, 2. increased hydrophobicity of the protein core, and 3. substitution of thermolabile residues exposed to the solvent
660469
additional information
Q86LS9
stable up to 45C
676982
additional information
-
the enzyme shows high thermostability
719472
additional information
Q58992
the crystal structure of archaeal serine hydroxymethyltransferase reveals idiosyncratic features likely required to withstand high temperatures
730918
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
glycine betaine protects the ApSHMT enzyme activity in vitro
I7H6W6
bsSHMT has six unconserved lysine residues in C-terminal domain which render it more resistant to alkaline denaturation. Chemical modification of lysine side chains results in stabilization of monomers
-
unlike the wild-type enzyme bsSHMT, which undergoes dissociation of native dimer into monomers at low guanidinium chloride concentrations, resulting in a non-cooperative unfolding of the enzyme, its chimera bsbstc, having the C-terminal domain of bstSHMT is resistant to low guanidinium chloride concentration and shows a guanidinium-chloride-induced cooperative unfolding from native dimer to unfolded monomer. The wild-type dimeric bstSHMT is resistant to low guanidinium chloride concentrations and shows a guanidinium chloride-induced cooperative unfolding, whereas its chimera bstbsc, having the C-terminal domain of bsSHMT, shows dissociation of native dimer into monomer at low guanidinium chloride concentrations and a guanidinium-induced non-cooperative unfolding. The C-terminal domain of dimeric SHMT plays a vital role in stabilization of the oligomeric structure of the native enzyme hence modulating its unfolding pathway
-
L-serine stabilizes
-
2-mercaptoethanol stabilizes
-
DTT stabilizes
-
EDTA stabilizes
-
pyridoxal 5'-phosphate stabilizes
-
above 6 M urea the dichrpoic activity is reduced significantly with a transition midpoint at 2.56 M. This process is completely reversible
-
guanidinium chloride-induced two-step unfolding of SHM1 with the first step being dissociation of dimer into apomonomer at low denaturant concentrations followed by unfolding of the stabilized monomer at higher denaturant concentrations, SHM1
P9WGI7, P9WGI9
guanidinium chloride-induced two-step unfolding of SHM1 with the first step being dissociation of dimer into apomonomer at low denaturant concentrations followed by unfolding of the stabilized monomer at higher denaturant concentrations, SHM2
P9WGI7, P9WGI9
urea-induced two-step unfolding of SHM1 with the first step being dissociation of dimer into apomonomer at low denaturant concentrations followed by unfolding of the stabilized monomer at higher denaturant concentrations. The enzyme-bound pyridoxal 5'-phosphate gets dissociated from the enzyme on treatment with about 1.25 M urea, SHM1
P9WGI7, P9WGI9
urea-induced two-step unfolding of SHM1 with the first step being dissociation of dimer into apomonomer at low denaturant concentrations followed by unfolding of the stabilized monomer at higher denaturant concentrations. The enzyme-bound pyridoxal 5'-phosphate gets dissociated from the enzyme on treatment with about 1.25 M urea, SHM2
P9WGI7, P9WGI9
the kcat value of the enzyme in phosphate buffer is about 60% of that measured in HEPES buffer
-
DTT stabilizes
-
pyridoxal 5'-phosphate stabilizes
-
folate stabilizes
-
2-mercaptoethanol stabilizes
-
dialysis inactivates
-
EDTA stabilizes
-
KCl, NaCl or LiCl: denaturation, folate protects
-
L-serine stabilizes
-
tetrahydrofolate stabilizes
-
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20 or -80C, 10% glycerol, for at least 6 months
Q2TL58
-20C (or -80C), in the presence of 10% glycerol, for at least 6 months, no significant change in catalytic activity
-
-20C, 8 weeks
-
-20C, 6-8 months in the presence of pyridoxal 5'-phosphate, 2-mercaptoethanol, DTT and EDTA
-
0C, at least 2 months in the presence of pyridoxal 5'-phosphate, 2-mercaptoethanol, DTT and EDTA
-
5C, precipitation after several days
-
frozen, several months at pH 7.3
-
-10C, 50% loss of activity in 10 h
-
4C, 50% loss of activity in 10 h
-
frozen, up to a month in the presence of 30% v/v glycerol
-
glycerol, 30% v/v, enhances thermal stability
-
4C, 8 weeks in the presence of folate
-
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
recombinant enzyme from Escherichia coli
I7H6W6
chimeric enzymes
-
the pyridoxal-5'-phosphate-binding domain of SHMT is purified from inclusion bodies by rapid mixing followed by MonoQ column chromatography
-
three-step purification, gel filtration, 14.8fold, more than 95% pure
Q2TL58
using a 30 to 50% ammonium sulfate precipitation, gel filtration and chromatography on CM-Sephadex columns. From 2 liters of cells, approximately 43 mg of pure zmSHMT is obtained with an overall yield of 90%
A9LDD9, Q7SXN1
DEAE-Sepharose column chromatography and Phenyl-Sepharose column chromatography
-
gel filtration
-
affinity chromatography on L-adsorbent
-
ammonium sulfate precipitation and DEAE-cellulose column chromatography
-
ammonium sulfate precipitation, DEAE-cellulose column chromatography, gel filtration
Q7SIB6
gene cloned and expressed in Escherichia coli
-
by ammonium sulfate precipitation and gel filtration, more than 95% pure
-
recombinant enzyme
-
recombinant enzymes by tandem affinity purification, immunoprecipitation, heat treatment,
-
partial by chloroplast preparation
-
by Ni2+-NTA affinity chromatography, 95% pure; using Ni-NTA chromatography
Q86LS9
heat-denaturation omitted
-
recombinant enzyme
-
SHM1; SHM2
P9WGI7, P9WGI9
by ammonium sulfate precipitation and gel filtration, more than 95% pure
-
recombinant enzyme
-
partial by chloroplast preparation
-
Ni-Sepharose column chromatography, Sephadex G-25 gel filtration, and SP-Sepharose column chromatography
-
the His-tagged enzyme is purified by His GraviTrap column chromatography, phenyl Sepharose column chromatography, and Superdex 200 gel filtration
-
DEAE-Sepharose column chromatography, SP-Sepharose column chromatography, and Sephadex G-25 gel filtration
-
affinity chromatography on L-adsorbent Sepharose
-
recombinant enzyme
-
by affinity chromatography
-
by Ni affinity chromatography, more than 98% pure
-
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
DNA and amino acid sequence determination and analysis, overexpression in Escherichia coli resulting in the increased accumulation of glycine and L-serine. Choline and glycine betaine levels are also significantly increased. Under high salinity, the growth rate of ApSHMT-expressing cells is faster compared to its respective control
I7H6W6
phylogenetic analysis, expression in Escherichia coli strain Rosetta, transient expression of EGFP-tagged full-length AtSHMT3 in Arabidopsis thaliana leaf protoplasts
Q94JQ3
expressed in Escherichia coli BL21(DE3) cells
-
expression of wild-type and chimeric mutant in Escherichia coli strain BL21 (DE3)
-
expressed in Escherichia coli
A9LDD9, Q7SXN1
into pET43.1a vector and transformed into Escherichia coli HMS174(DE3) cells
Q2TL58
Escherichia coli DH5alpha-PUC19 and Escherichia coli BL21 (DE3) used as host-vector system
-
Escherichia coli glyA gene
-
expressed in Escherichia coli strain GS1993 recA-
-
expression in Escherichia coli strain BL21 (DE3)
-
using the AlkS/PalkB-expression system Escherichia colis serine hydroxymethyltransferase gene glyA is overexpressed in Escherichia coli. It is shown that the system is already fully turned on at inducer concentrations as low as 0.005% (v/v). The optimum induction procedure for production of serine hydroxymethyltransferase is elaborated. Volumetric and specific productivity are found to increase with specific growth rate in glucose-limited fed-batch cultures. Acetate excretion as a result of recombinant protein production can be avoided in an optimized fermentation protocol by switching earlier to a linear feed. A final cell dry weight (CDW) concentration of 52 g/l is reached producing recombinant GlyA with a maximum specific activity of 6.3 U/mg total protein
-
expressed in Escherichia coli BL21(DE3) cells
-
expression in Escherichia coli
-
expression of wild-type and chimeric mutant in Escherichia coli strain BL21 (DE3)
-
expression in Escherichia coli
-
expression of a dominant negative, tetracycline-inducible SHMT1 protein, DN2-SHMT1, in HeLa and SH-SY5Y cells, expression of RFP-tagged SHMT2alpha and of YFP- or FLAG-tagged SHMT1
-
into the pGL3 vector and transfected into MCF-7 cells
-
mutations introduced into the cDNA for human cytosolic SHMT and expressed from an Escherichia coli expression system
-
phylogenetic analysis, expression in Escherichia coli strain Rosetta
-
gene HTH1832, overexpression in Escherichia coli
-
expressed as a His-tagged fusion protein in Escherichia coli; into pQE60 vector having C terminal His6-tag, expression in Escherichia coli M15 cells
Q86LS9
both isoforms cloned in frame with EGFP at their C-terminus and transfected into Leishmania major
-
expression in Escherichia coli
-
heterologously overproduced in Escherichia coli without a His6-tag
-
SHM1; SHM2
P9WGI7, P9WGI9
expression in Escherichia coli
-
mutations introduced into the cDNA for rabbit cytosolic SHMT and expressed from an Escherichia coli expression system
-
expression in Escherichia coli
-
wild-type and mutant enzymes S52A, S52C and R262A are overexpressed in Escherichia coli
-
expressed in Escherichia coli BL21(DE3) and GS245(DE3) cells
-
genes pfshmt and PF14_ 0534, encoding isozymes PfSHMTc and PfSHMTm, respectively, DNA and amino acid sequence determination and analysis, recombinant expression of His-tagged full-length isozymes
-
His6-tagged enzyme is expressed in Escherichia coli BL21-CodonPlus (DE3)-RIL cells
-
expressed in Escherichia coli
A5K8L9
expressed in Escherichia coli BL21(DE3) cells
-
full-length cDNA clone SST18 encoding potato SHMT inserted in antisense orientation into the pBIN19 based vector L700 and introduced into the genome of Solanum tuberosum
-
expressed as fusion protein with an N-terminal Strep-tag in Escherichia coli strain BL21 Gold
-
wild-type and mutants cloned into vector pET-29B and expressed in Escherichia coli BL21(DE3) cells, moreover expressed in Trichomonas vaginalis with a C-terminal HA tag
-
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
high salinity also strongly induces the transcript level of ApSHMT in Aphanothece halophytica
I7H6W6
in mitochondria, ferredoxin-dependent glutamate synthase interacts physically with SHMT1, and this interaction is necessary for photorespiratory SHMT activity
-
about 3fold increase of SHMT activity during exponential growth with a further increase at the onset of the stationary phase, the essential SHMT has highest activity in the stationary phase and the regulator GlyR acts as an activator of transcription in this growth phase. Addition of glycine results in a slight but significant increase of SHMTactivity by 75%
-
about 3fold increase of SHMT activity during exponential growth with a further increase at the onset of the stationary phase, the essential SHMT has highest activity in the stationary phase and the regulator GlyR acts as an activator of transcription in this growth phase. Addition of glycine results in a slight but significant increase of SHMTactivity by 75%
Corynebacterium glutamicum ATCC13032
-
-
a non-lethal dose of UV-C radiation (10 mJ/cm2 UV (254 nm)) increases SHMT1 internal ribosome entry site activity and protein levels
-
heterogeneous nuclear ribonucleoprotein H2 stimulates SHMT1 internal ribosome entry site activity by binding to the 5-untranslated region of the transcript and interacting with CUG-binding protein 1, CUG-binding protein 1 stimulates the internal ribosome entry site-mediated translation of SHMT1
-
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
L276A
-
the mutant is in the monomeric state and shows reduced activity
L276A
-
the mutation has the effect of lowering the cooperativity of urea denaturation process
L276A
-
site-directed mutagenesis, mutation in the third hydrophobic cluster. The decrease of hydrophobic contact area in the mutant causes a shift of the equilibrium between dimeric and monomeric forms in favor of the latter, pyridoxal 5'-phosphate binding stabilizes the dimeric form of the mutant
L785A/L276A
-
the mutation has the effect of lowering the cooperativity of urea denaturation process
L85A
-
the apo-L85A mutant enzyme is approximately 75% dimeric and shows reduced activity
L85A
-
the mutation affect the quaternary structure stability of SHMT
L85A
-
site-directed mutagenesis, mutation in the third hydrophobic cluster. The decrease of hydrophobic contact area in the mutant causes a shift of the equilibrium between dimeric and monomeric forms in favor of the latter, pyridoxal 5'-phosphate binding stabilizes the dimeric form of the mutant
L85A/L276A
-
the mutant is in the monomeric state and shows reduced activity
P214A
-
the turnover-number is 1.5fold lower than the wild-type value, the Km-value for Ser is 2.1fold lower than the wild-type value, The Km-value for tetrahydropteroylglutamate is 1.3fold higher than the wild-type value, Tm-value in absence of Ser is 3.5C lower than the wild-type Tm-value. The Tm-value in presence of Ser is 4C higher than the wild-type value
P214G
-
the turnover-number is 1.5fold lower than the wild-type value, the Km-value for Ser is 1.3fold lower than the wild-type value, The Km-value for tetrahydropteroylglutamate is 1.3fold higher than the wild-type value
P216A
-
the turnover-number is 1.5fold lower than the wild-type value, the Km-value for Ser is 1.2fold lower than the wild-type value. The Km-value for tetrahydropteroylglutamate is 1.3fold higher than the wild-type value, Tm-value in absence of Ser is 3.5C higher than the wild-type Tm-value, The Tm-value in presence of Ser is 0.5C higher than the wild-type value
P216G
-
the turnover-number is 8.3fold lower than the wild-type value, the Km-value for Ser is 1.9fold higher than the wild-type value. The Km-value for tetrahydropteroylglutamate is 5.7fold higher than the wild-type value
P218A
-
the turnover-number is 1.1fold lower than the wild-type value, the Km-value for Ser is 2.3fold lower than the wild-type value. The Km-value for tetrahydropteroylglutamate is 1.3fold higher than the wild-type value, double thermal transition that is considerably lower than wild-type enzyme, no increase in thermal stability upon binding serine
P218G
-
the turnover-number is 1.5fold lower than the wild-type value, the Km-value for Ser is 2.3fold lower than the wild-type value. The Km-value for tetrahydropteroylglutamate is 1.1fold higher than the wild-type value
P258A
-
the turnover-number is below 0.5 per min, the KM-value for Ser is 26.7fold higher than the wild-type value
P258G
-
inactive mutant enzyme
P264A
-
the turnover-number is 3fold lower than the wild-type value, the Km-value for Ser is 1.1fold higher than the wild-type value, The Km-value for tetrahydropteroylglutamate is 1.1fold higher than the wild-type value, Tm-value in absence of Ser is 9C lower than the wild-type Tm-value. The Tm-value in presence of Ser is 11.5C lower than the wild-type value
E53Q
-
site-directed mutagenesis, mutation of a substrate binding residue, the mutant retains tetrahydrofolate-independent aldolase activity
F351G
Q7SIB6
the mutation has no effect on tetrahydrofolate-independent and tetrahydrofolate-dependent activities
K226M
-
mutant enzymes is inactive, drastic rate of formation of the quinoid intermediate. It contains 1 mol of pyridoxal 5'-phosphate per mol of subunit. pyridoxal 5'-phosphate is bound at the active site in an orientation different from that of the wild-type enzyme. K-226 is responsible for flipping of pyridoxal 5'-phosphate from one orientation to another which is crucial for tetrahydropteroylglutamate-dependent Calpha-Cbeta bond cleavage of L-Ser
N341A
Q7SIB6
the mutant is inactive for the tetrahydrofolate-dependent activity, while the mutation has no effect on tetrahydrofolate-independent activity
Y51F
-
the mutation results in a complete loss of tetrahydrofolate-dependent and tetrahydrofolate-independent activities
Y60A
Q7SIB6
the mutant is inactive for the tetrahydrofolate-dependent activity, while the mutation has no effect on tetrahydrofolate-independent activity
Y61A
-
the mutation results in a complete loss of tetrahydrofolate-dependent and tetrahydrofolate independent activities
Y61A
-
site-directed mutagenesis, the bsSHMT mutant has lost aldolase activity to L-allo-threonine
Y61F
-
site-directed mutagenesis, the bsSHMT mutant has lost aldolase activity to L-allo-threonine
S394N
-
shows normal values for kcat and Km for serine, has increased dissociation constant values for both glycine and tetrahydrofolate and its pentaglutamate form compared to wild-type enzyme, decreased rates of pyridoxal phosphate addition to the mutant apo enzymes to form the active holo enzymes, thermal stability of SHMT or the rate at which it converts 5,10-methenyl tetrahydropteroyl pentaglutamate to 5-formyl tetrahydropteroyl pentaglutamate not affected
E75L
-
no activity with L-Ser and tetrahydrofolate. The mutant enzyme does not catalyze the formation of 5,10-methenyl-tetrahydropteroylglutamate or N5-hydroxymethylene-tetrahydropteroylglutamate
E75L
-
site-directed mutagenesis, mutation of a substrate binding residue, the mutant retains tetrahydrofolate-independent aldolase activity
E75Q
-
500fold decrease in activity with L-Ser and tetrahydrofolate compared to wild-type enzyme, the KM-value for L-allothreonine is 10fold increased compared to wild-type value, the turnover-number for reaction with L-allothreonine is 4.3fold increased compared to wild-type enzyme
E75Q
-
site-directed mutagenesis, mutation of a substrate binding residue, the mutant retains tetrahydrofolate-independent aldolase activity
L474F
-
shows normal values for kcat and Km for serine, shows lowered affinity (increased dissociation constant) for only the pentaglutamate form of the folate ligand, shows decreased rates of pyridoxal phosphate addition to the mutant apo enzymes to form the active holo enzymes, thermal stability of SHMT or the rate at which it converts 5,10-methenyl tetrahydropteroyl pentaglutamate to 5-formyl tetrahydropteroyl pentaglutamate not affected
S394N
-
shows normal values for kcat and Km for serine, has increased dissociation constant values for both glycine and tetrahydrofolate and its pentaglutamate form compared to wild-type enzyme, shows decreased rates of pyridoxal phosphate addition to the mutant apo enzymes to form the active holo enzymes, thermal stability of SHMT or the rate at which it converts 5,10-methenyl tetrahydropteroyl pentaglutamate to 5-formyl tetrahydropteroyl pentaglutamate not affected
C203S
-
no loss of activity
D227N
-
nearly complete loss of activity, enzyme exists as dimer
E74K
-
specific activities drastically reduced with serine as substrate, but D-alanine transamination and allothreonine cleavage at rates comparable with wild-type enzyme
E74Q
-
specific activities drastically reduced with serine as substrate, but D-alanine transamination and allothreonine cleavage at rates comparable with wild type enzyme
E74Q
-
site-directed mutagenesis, mutation of a substrate binding residue, the mutant retains tetrahydrofolate-independent aldolase activity
H147N
-
site-directed mutagenesis, mutation of a substrate binding residue, the mutant retains tetrahydrofolate-independent aldolase activity
H230Y
-
90% loss of enzyme activity, confers ability to oxidize NADH
H304A
-
nearly complete loss of activity, enzyme exists as dimer
H306A
-
partial loss of activity, 60% of the enzyme exists as dimer
H356A
-
partial loss of activity, 80% of the enzyme exists as dimer
K71Q
-
nearly complete loss of activity, enzyme exists as dimer
P297R
-
85-90% loss of enzyme activity
R262A
-
KM-value for L-Ser is 5.2fold higher than the wild-type value, the turnover-number is 5.25fold lower than the wild-type value, no transamination reaction with D-Ala, reaction with L-allo-Thr is 20fold decreased compared to wild-type value. L-Ser is unable to enhance the thermal stability as it does in wild-type enzyme
R80A
-
nearly complete loss of activity, enzyme exists as dimer
R98A
-
mutant enzyme is present in the insoluble fraction
S202C
-
partial loss of activity, 55% of the enzyme exists as dimer
S52A
-
KM-value for L-Ser is 1.3fold higher than the wild-type value, the turnover-number is 6fold lower than the wild-type value, transamination reaction with D-Ala is 20% of the wild-type activity, reaction with L-allo-Thr is 15% of the wild-type activity. L-Ser is unable to enhance the thermal stability as it does in wild-type enzyme
S52C
-
KM-value for L-Ser is 11.2fold higher than the wild-type value, the turnover-number is 21fold lower than the wild-type value, no transamination reaction with D-Ala, no reaction with L-allo-Thr. L-Ser is unable to enhance the thermal stability as it does in wild-type enzyme
W110A
-
mutant enzyme is present in the insoluble fraction
W110F
-
no loss of activity
Y72F
-
partial loss of activity, 30% of the enzyme exists as dimer
Y81F
-
20% of the enzyme exists as dimer
K251Q
-
oligomeric structure not affected, but inactive in both the presence and absence of pyridoxal phosphate
K251R
-
oligomeric structure not affected, catalytic activity in the presence of pyridoxal phosphate also unaffected
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
additional information
-
construction of chimeric enzymes by swapping the structural domains between the bsSHMT from Bacillus subtilis and the bstSHMT frok Bacillus stearothermophilus and generation of the two chimeric proteins bsbstc and bstbsc. The chimeras have secondary structure, tyrosine and pyridoxal 5'-phosphate microenvironment similar to that of the wild-type proteins. The chimeras show enzymatic activity slightly higher than that of the wild-type proteins.Unlike the wild-type enzyme bsSHMT, which undergoes dissociation of native dimer into monomers at low guanidinium chloride concentrations, resulting in a non-cooperative unfolding of the enzyme, its chimera bsbstc, having the C-terminal domain of bstSHMT is resistant to low guanidinium chloride concentration and shows a guanidinium-chloride-induced cooperative unfolding from native dimer to unfolded monomer. The wild-type dimeric bstSHMT is resistant to low guanidinium chloride concentrations and shows a guanidinium chloride-induced cooperative unfolding, whereas its chimera bstbsc, having the C-terminal domain of bsSHMT, shows dissociation of native dimer into monomer at low guanidinium chloride concentrations and a guanidinium-induced non-cooperative unfolding
additional information
-
generation of a chimera from Bacillus stearothermophilus and Bacillus subtilis SHMTs by domain swapping, quarternary structure analysis, overview
additional information
-
SHMT activity controlled by Ptac, greatly reduced SHMT activity if no isopropyl-thio-beta-D-galactopyranoside is present, is explicitly prone to chromosomal mutations and rearrangements, thus making the strain unsuitable for large-scale fermentations
L85A/L276A
-
site-directed mutagenesis, mutation in the third hydrophobic cluster. The decrease of hydrophobic contact area in the mutant causes a shift of the equilibrium between dimeric and monomeric forms in favor of the latter, pyridoxal 5'-phosphate binding stabilizes the dimeric form of the mutant
additional information
-
mutant strain 1D19 from first round of DNA-shuffling, shows a 1.7fold increase in SHMT activity, mutant strain 2G31 from the second round of shuffling shows a 2.8fold increase in SHMT activity, mutant strain 3E7 from third round of shuffling, approximately 8fold increased enzyme activity and 41fold increased enzyme productivity as compared with its wild-type parent
additional information
-
immobilization of cells using 3% alginate (w/v), 5 g cells (wet), and 2% (w/v) CaCl2 solution
P264G
-
the turnover-number is 42.9fold lower than the wild-type value, the Km-value for Ser is 4.4fold higher than the wild-type value
additional information
Escherichia coli AB90054
-
mutant strain 1D19 from first round of DNA-shuffling, shows a 1.7fold increase in SHMT activity, mutant strain 2G31 from the second round of shuffling shows a 2.8fold increase in SHMT activity, mutant strain 3E7 from third round of shuffling, approximately 8fold increased enzyme activity and 41fold increased enzyme productivity as compared with its wild-type parent
-
additional information
Escherichia coli K-12 MG1655
-
immobilization of cells using 3% alginate (w/v), 5 g cells (wet), and 2% (w/v) CaCl2 solution
-
K226Q
-
mutant enzymes is inactive, drastic rate of formation of the quinoid intermediate. It contains 1 mol of pyridoxal 5'-phosphate oer mol of subunit. pyridoxal 5'-phosphate is bound at the active site in an orientation different from that of the wild-type enzyme. K-226 is responsible for flipping of pyridoxal 5'-phosphate from one orientation to another which is crucial for tetrahydropteroylglutamate-dependent Calpha-Cbeta bond cleavage of L-Ser
additional information
-
construction of chimeric enzymes by swapping the structural domains between the bsSHMT from Bacillus subtilis and the bstSHMT from Bacillus stearothermophilus and generation of the two chimeric proteins bsbstc and bstbsc. The chimeras have secondary structure, tyrosine and pyridoxal 5'-phosphate microenvironment similar to that of the wild-type proteins. The chimeras show enzymatic activity slightly higher than that of the wild-type proteins.Unlike the wild-type enzyme bsSHMT, which undergoes dissociation of native dimer into monomers at low guanidinium chloride concentrations, resulting in a non-cooperative unfolding of the enzyme, its chimera bsbstc, having the C-terminal domain of bstSHMT is resistant to low guanidinium chloride concentration and shows a guanidinium-chloride-induced cooperative unfolding from native dimer to unfolded monomer. The wild-type dimeric bstSHMT is resistant to low guanidinium chloride concentrations and shows a guanidinium chloride-induced cooperative unfolding, whereas its chimera bstbsc, having the C-terminal domain of bsSHMT, shows dissociation of native dimer into monomer at low guanidinium chloride concentrations and a guanidinium-induced non-cooperative unfolding
additional information
-
generation of a chimera from Bacillus stearothermophilus and Bacillus subtilis SHMTs by domain swapping, quarternary structure analysis, overview
L474F
-
shows normal values for kcat and Km for serine, shows lowered affinity (increased dissociation constant) for only the pentaglutamate form of the folate ligand, decreased rates of pyridoxal phosphate addition to the mutant apo enzymes to form the active holo enzymes, thermal stability of SHMT or the rate at which it converts 5,10-methenyl tetrahydropteroyl pentaglutamate to 5-formyl tetrahydropteroyl pentaglutamate not affected
additional information
-
mutation of the consensus metal regulatory element sequence decreases the promoter activity of the -219 to -1 fragment by 60% in the absence of L-mimosine and attenuates L-mimosine inhibition by nearly 40%, mutation of the NF1 consensus sequence in the SHMT1 promoter -219 to -1 partially attenuates L-mimosine inhibition by ca. 20% without influencing SHMT1 promoter activity
Y82F
-
95% loss of activity, kcat and Km decreased, a role in stabilizing the quinonoid intermediate
additional information
A5K8L9
sequencing of 12 Plasmodium vivax SHMT isolates reveals limited polymorphisms in 3 noncoding regions
additional information
-
SHMT mutant with only partial segregation
Renatured/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
5 ml of supernatant containing the solubilized domain is added drop by drop to 100 ml of stirring potassium phosphate buffer (50 mM, pH 7.4 containing 1 mM EDTA, 2 mM beta-mercaptoethanol, 0.1 mM pyridoxal 5'-phosphate, and 0.1 M NaCl)
-
denatured SHMT samples (0.023 mM in 8 M urea at 20C) are able to recover after 4 h when kept with 8 M urea in 50 mM Na-HEPES, pH 7.2, containing 0.2 mM dithiothreitol and 0.1 mM EDTA for 15 h at 20C
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pharmacology
-
L-serine is required for pharmaceutical purposes, availability of a sugar-based microbial process for its production is desirable, however, SHMT prevents overproduction of L-serine, control of the essential SHMT activity by a novel physiological approach
medicine
Q2TL58
animal model for drug screening of SHMT
medicine
Danio rerio AB
-
animal model for drug screening of SHMT
-
biotechnology
-
the AlkS/PalkB-expression system is shown as an efficient tool for the production of recombinant serine hydroxymethyltransferase in Escherichia coli fed-batch fermentations
medicine
-
enzyme is a potential target for cancer chemotherapy
medicine
-
enzyme is a target for antibiotics
synthesis
-
improved method for preparation of optically pure beta-hydroxy-alpha-amino acids, catalyzed by serine hydroxymethyl transferase with threonine aldolase activity. Usage of substrates beta-phenylserine, beta-(nitrophenyl) serine and beta-(methylsulfonylphenyl) serine with immobilized recombinant enzyme for SHMT activity, optimal at pH 7.5 and 45C. The immobilized cells are continuously used 10 times, yielding an average conversion rate of 60.4%
synthesis
Escherichia coli K-12 MG1655
-
improved method for preparation of optically pure beta-hydroxy-alpha-amino acids, catalyzed by serine hydroxymethyl transferase with threonine aldolase activity. Usage of substrates beta-phenylserine, beta-(nitrophenyl) serine and beta-(methylsulfonylphenyl) serine with immobilized recombinant enzyme for SHMT activity, optimal at pH 7.5 and 45C. The immobilized cells are continuously used 10 times, yielding an average conversion rate of 60.4%
-
medicine
-
enzyme is a potential target for cancer chemotherapy
analysis
P34896
molecular dynamics simulations and interaction energy analysis for compounds designed as potential selective inhibitors of Plasmodium falciparum SHMT based on the conformational and dynamics differences observed between the residues Asp146 and Glu137 in the active sites of human SHMT and Plasmodium falciparum SHMT, respectively
analysis
-
SHMT1 is a zinc-inducible gene, provides first mechanism for the regulation of folate-mediated one-carbon metabolism by zinc
medicine
-
enzyme is a potential target for cancer chemotherapy
medicine
-
the cytosolic SHMT is a target enzyme for chemotherapy
medicine
Q86LS9
drug target in Leishmania, ldSHMT is of medical importance as a drug target since ldSHMT is preferentially expressed in the amastigote stage of parasite which resides in human macrophages
medicine
Leishmania donovani MHOM/IN/80/Dd8
-
drug target in Leishmania, ldSHMT is of medical importance as a drug target since ldSHMT is preferentially expressed in the amastigote stage of parasite which resides in human macrophages
-
analysis
-
protein sequence of the two isoforms, the short form SHMT-S and the long form SHMT-L, show 59% identity
medicine
-
enzyme is a potential target for cancer chemotherapy
medicine
-
enzyme is a potential target for cancer chemotherapy
medicine
-
enzyme is a potential target for cancer chemotherapy
analysis
-
molecular dynamics simulations and interaction energy analysis for compounds designed as potential selective inhibitors of Plasmodium falciparum SHMT based on the conformational and dynamics differences observed between the residues Asp146 and Glu137 in the active sites of human SHMT and Plasmodium falciparum SHMT, respectively
medicine
-
SHMT is a potential target for antimalarial chemotherapy
medicine
Plasmodium falciparum strainTM4
-
SHMT is a potential target for antimalarial chemotherapy
-
degradation
-
essential for one-carbon metabolism
medicine
-
enzyme is a potential target for cancer chemotherapy
additional information
Q49K94
two conserved inserts of 3 and 31 amino acids, distinctive characteristics of the Chlamydiales order, ancient lateral gene transfers from actinobacteria to chlamydiae
medicine
-
enzyme is distinct from its prokaryotic and eukaryotic counterparts, thus is a potential drug target
additional information
Q49KA1
two conserved inserts of 3 and 31 amino acids, distinctive characteristics of the Chlamydiales order, ancient lateral gene transfers from actinobacteria to chlamydiae