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Information on EC 2.1.2.1 - glycine hydroxymethyltransferase and Organism(s) Homo sapiens and UniProt Accession P34896

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IUBMB Comments
A pyridoxal-phosphate protein. Also catalyses the reaction of glycine with acetaldehyde to form L-threonine, and with 4-trimethylammoniobutanal to form 3-hydroxy-N6,N6,N6-trimethyl-L-lysine.
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Homo sapiens
UNIPROT: P34896
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Word Map
The taxonomic range for the selected organisms is: Homo sapiens
The enzyme appears in selected viruses and cellular organisms
Synonyms
serine hydroxymethyltransferase, shmt2, shmt1, serine hydroxymethyl transferase, serine transhydroxymethylase, serine hydroxymethyltransferase 2, mitochondrial serine hydroxymethyltransferase, serine hydroxymethyltransferase 1, bsshmt, pvshmt, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
serine hydroxymethyltransferase
-
SHMT1
SHMT2alpha
-
hSHMT
-
-
L-serine hydroxymethyltransferase
-
-
-
-
mitochondrial serine hydroxymethyltransferase
-
serine hydroxymethylase hydroxymethyltransferase, serine
-
-
-
-
serine hydroxymethyltransferase
serine hydroxymethyltransferase 1
-
-
serine hydroxymethyltransferase 2
-
-
serine hydroxymethyltransferase 2alpha
-
-
serine transhydroxymethylase
-
-
-
-
SHMT2
SHMT2alpha
-
-
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
5,10-methylenetetrahydrofolate + glycine + H2O = tetrahydrofolate + L-serine
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydroxymethyl group transfer
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
5,10-methylenetetrahydrofolate:glycine hydroxymethyltransferase
A pyridoxal-phosphate protein. Also catalyses the reaction of glycine with acetaldehyde to form L-threonine, and with 4-trimethylammoniobutanal to form 3-hydroxy-N6,N6,N6-trimethyl-L-lysine.
CAS REGISTRY NUMBER
COMMENTARY hide
9029-83-8
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
(6S)-tetrahydrofolate + D-serine
5,10-methylenetetrahydrofolate + glycine + H2O
show the reaction diagram
poor activity
-
-
r
(6S)-tetrahydrofolate + L-serine
5,10-methylenetetrahydrofolate + glycine + H2O
show the reaction diagram
-
-
-
r
5,10-methylenetetrahydrofolate + glycine + H2O
tetrahydrofolate + L-serine
show the reaction diagram
tetrahydrofolate + L-serine
5,10-methylenetetrahydrofolate + glycine + H2O
show the reaction diagram
5,10-methenyl-tetrahydropteroyl pentaglutamate + glycine + H2O
5-formyl-tetrahydropteroyl pentaglutamate + L-serine
show the reaction diagram
-
-
-
-
?
5,10-methylenetetrahydrofolate + glycine + H2O
tetrahydrofolate + L-serine
show the reaction diagram
alpha-methylserine + tetrahydrofolate
D-alanine + 5,10-methylenetetrahydrofolate
show the reaction diagram
-
-
-
-
?
L-Ser + tetrahydrofolate
Gly + 5,10-methylenetetrahydrofolate
show the reaction diagram
-
-
-
-
r
L-serine + tetrahydrofolate
glycine + 5,10-methylenetetrahydrofolate + H2O
show the reaction diagram
tetrahydrofolate + L-serine
5,10-methylenetetrahydrofolate + glycine + H2O
show the reaction diagram
additional information
?
-
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
(6S)-tetrahydrofolate + L-serine
5,10-methylenetetrahydrofolate + glycine + H2O
show the reaction diagram
-
-
-
r
5,10-methylenetetrahydrofolate + glycine + H2O
tetrahydrofolate + L-serine
show the reaction diagram
tetrahydrofolate + L-serine
5,10-methylenetetrahydrofolate + glycine + H2O
show the reaction diagram
5,10-methylenetetrahydrofolate + glycine + H2O
tetrahydrofolate + L-serine
show the reaction diagram
L-serine + tetrahydrofolate
glycine + 5,10-methylenetetrahydrofolate + H2O
show the reaction diagram
tetrahydrofolate + L-serine
5,10-methylenetetrahydrofolate + glycine + H2O
show the reaction diagram
additional information
?
-
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
5,10-methylenetetrahydrofolate
-
pyridoxal 5'-phosphate
tetrahydrofolate
-
pyridoxal 5'-phosphate
tetrahydrofolate
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
3-Bromopyruvate
isoform SHMT1 is completely inhibited by 3-bromopyruvate
tetrahydrofolate
Thiosemicarbazide
-
3-Bromopyruvate
isoform SHMT2 retains a significant fraction of activity with 3-bromopyruvate
4-chloro-L-threonine
-
-
beta-trifluoroallothreonine
-
-
beta-trifluorothreonine
-
-
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
lometrexol
methotrexate
nolatrexed
-
poor inhibition
pemetrexed
raltitrexed
substituted hydroxylamine derivates
-
-
-
sulfonyl fluoride triazine derivates
-
-
tetrahydrofolate
Thiosemicarbazide
-
-
additional information
prototypes with negative total charge have greater affinity for Plasmodium falciparum SHMT than for human SHMT
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
pyridoxal 5'-phosphate
-
-
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 hide
LITERATURE
IMAGE
0.0052 - 0.021
(6S)-tetrahydrofolate
0.291
5,10-methylenetetrahydrofolate
isoform SHMT1, at pH 8.8 and 30°C
55
D-serine
pH 7.0, 25°C, recombinant enzyme
0.556
glycine
isoform SHMT1, at pH 8.8 and 30°C
0.1 - 4.8
L-serine
0.02 - 0.033
tetrahydrofolate
0.98
5,10-methylenetetrahydrofolate
isoform SHMT2, at pH 8.8 and 30°C
0.66
glycine
isoform SHMT2, at pH 8.8 and 30°C
0.15 - 2.2
L-serine
0.0037 - 0.223
tetrahydrofolate
additional information
additional information
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.188
glycine
isoform SHMT1, at pH 8.8 and 30°C
2 - 15
L-serine
6.23 - 9.58
tetrahydrofolate
9.58 - 30
L-serine
0.02 - 30
tetrahydrofolate
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.65
5,10-methylenetetrahydrofolate
isoform SHMT1, at pH 8.8 and 30°C
0.172
D-serine
pH 7.0, 25°C, recombinant enzyme
0.33
glycine
isoform SHMT1, at pH 8.8 and 30°C
1.33 - 155.5
L-serine
188.83
tetrahydrofolate
isoform SHMT1, at pH 7.2 and 30°C
0.52
5,10-methylenetetrahydrofolate
isoform SHMT2, at pH 8.8 and 30°C
0.77
glycine
isoform SHMT2, at pH 8.8 and 30°C
6.5 - 123
L-serine
63.5 - 6000
tetrahydrofolate
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.368
L-serine
isoform SHMT1, at pH 7.2 and 30°C
0.258
tetrahydrofolate
isoform SHMT1, at pH 7.2 and 30°C
0.602
L-serine
isoform SHMT2, at pH 7.8 and 30°C
0.023
lometrexol
-
at pH 7.2 and 30°C
0.201
methotrexate
-
at pH 7.2 and 30°C
1
nolatrexed
-
Ki above 1 mM, at pH 7.2 and 30°C
0.122
raltitrexed
-
at pH 7.2 and 30°C
0.14 - 0.27
tetrahydrofolate
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
10
-
recombinant enzyme
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.8
recombinant enzyme
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.6 - 8.4
-
the catalytic efficiency of the enzyme for tetrahydrofolate is about 29fold greater at pH 6.6 than at pH 8.3
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
25
assay at
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
3 - 43
activity range
additional information
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
expresses low levels of SHMT2
Manually annotated by BRENDA team
in healthy brains, SHMT2 expression is not detected in most cells but is at low levels in astrocytes and vessels
Manually annotated by BRENDA team
-
expression patterns of SHMT2 in 76 breast cancer patients after modified radical mastectomy, immunohistochemic analysis, SHMT2 is highly expressed in breast cancer cells, and the expression level of SHMT2 is positively correlated with breast cancer grade
Manually annotated by BRENDA team
expresses low levels of SHMT2
Manually annotated by BRENDA team
in human glioblastoma multiforme, mitochondrial serine hydroxymethyltransferase (SHMT2) and glycine decarboxylase are highly expressed in the pseudopalisading cells that surround necrotic foci
Manually annotated by BRENDA team
expression of SHMT2 in ischemic tumor zones
Manually annotated by BRENDA team
-
low activity, activity is similar 8 weeks post conception and at term
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
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
the enzyme belongs to the alpha class of PLP-dependent enzymes. The ligand binding environment of enzymes SHMT from human and Plasmodium are different, overview
physiological function
the enzyme dynamically changes the fluxes of one-carbon metabolism by reversibly converting L-serine and tetrahydrofolate into 5,10-methylene-tetrahydrofolate and glycine. The cytosolic isoforms can also translocate to the nucleus to sustain de novo thymidylate synthesis and support cell proliferation
malfunction
metabolism
physiological function
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
GLYC_HUMAN
483
0
53083
Swiss-Prot
other Location (Reliability: 1)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
195000
cytosolic isoform, gel filtration
52020
4 * 52020, cytosolic isoform, sequence calculation, 4 * 53000, recombinant cytosolic isoform, SDS-PAGE
53000
4 * 52020, cytosolic isoform, sequence calculation, 4 * 53000, recombinant cytosolic isoform, SDS-PAGE
additional information
-
review
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
homotetramer
4 * 52020, cytosolic isoform, sequence calculation, 4 * 53000, recombinant cytosolic isoform, SDS-PAGE
tetramer
dimer
-
-
dimer or tetramer
isoform SHMT2, X-ray crystallography
homotetramer
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
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
additional information
-
enzyme is a mRNA binding protein
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
mutant H135N/R137A/E168N, hanging drop vapor diffusion method, using 0.1 M sodium cacodylate pH 6.5, 1.0 M sodium citrate
holo- and apo-isoform SHMT2, hanging drop vapor diffusion method, using 0.1 M Bis/Tris propane pH 7.5, 5% (v/v) glycerol, 12-16% (w/v) poly(ethylene glycol) 3350, 0.2 M potassium fluoride
sitting drop vapor diffusion method, using 0.1 M Bis-Tris pH 6.5, 28% (w/v) PEGMME 2000 (in complex with lometrexol and methotrexate), 0.2 M LiCl2, 0.1 M MES pH 6.0, 20% (w/v) PEG6000 (in complex with pemetrexed), and 0.2 M NaCl, 0.1 M MES pH 6.0, 20% (w/v) PEG6000 (in complex with raltitrexed)
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
H135N/R137A
dimeric catalytically active mutant
H135N/R137A/E168N
tetrameric active mutant with a modified, less stable, tetrameric interface
K257Q/Y82A/Y83F
tetrameric inactive mutant
A206C
the mutation yields an enzyme that forms a 3-bromopyruvate-enzyme complex and is completely inactivated
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
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
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
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant enzyme 11.2fold from Escherichia coli strain BL21(DE3) to homogeneity by polyethyleneimine precipitation, anion exchange chromatography, and gel filtration
by ammonium sulfate precipitation and gel filtration, more than 95% pure
-
His-Trap column chromatography and Superdex 75 gel filtration
polyethyleneimine precipitation, Q-Sepharose column chromatography and Sephacyl S-200 gel filtration
-
recombinant enzyme
-
recombinant enzymes by tandem affinity purification, immunoprecipitation, heat treatment,
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli
expressed in Escherichia coli BL21(DE3) cells
recombinant soluble enzyme overexpression in Escherichia coli strain BL21(DE3)
expressed in Escherichia coli
expressed in Escherichia coli BL21(DE3) cells
expressed in Escherichia coli BL21(DE3)-TIR cells
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
-
expression pattern of SHMT2 in 76 breast cancer patients after modified radical mastectomy, expression analysis
-
gene SHMT2, expression analysis
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
-
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
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
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
drug development
the human enzyme is a potential target for cancer treatment
analysis
-
SHMT1 is a zinc-inducible gene, provides first mechanism for the regulation of folate-mediated one-carbon metabolism by zinc
drug development
the enzyme might be a a key target for the development of chemotherapic agents
medicine
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Kruschwitz, H.; Ren, S.; Di Salvo, M.; Schifch, V.
Expression, purification, and characterization of human cytosolic serine hydroxymethyltransferase
Protein Expr. Purif.
6
411-416
1995
Homo sapiens
Manually annotated by BRENDA team
Appaji Rao, N.; Talwar, R.; Savithri, H.S.
Molecular organization, catalytic mechanism and function of serine hydroxymethyltransferase - a potential target for cancer chemotherapy
Int. J. Biochem. Cell Biol.
32
405-416
2000
Saccharomyces cerevisiae, Oryctolagus cuniculus, Escherichia coli, Ovis aries, Homo sapiens, Pisum sativum
Manually annotated by BRENDA team
Ogawa, H.; Gomi, T.; Fujioka, M.
Serine hydroxymethyltransferase and threonine aldolase: are they identical?
Int. J. Biochem. Cell Biol.
32
289-301
2000
Cricetulus griseus, Escherichia coli, Homo sapiens, Neurospora crassa, Oryctolagus cuniculus, Ovis aries, Pisum sativum, Rattus norvegicus, Vigna radiata
Manually annotated by BRENDA team
Chave, K.J.; Snell, K.; Sanders, P.G.
Isolation and characterization of human genomic sequences encoding cytosolic serine hydroxymethyltransferase
Biochem. Soc. Trans.
25
53S
1997
Homo sapiens
Manually annotated by BRENDA team
Liu, X.; Reig, B.; Nasrallah, I.M.; Stover, P.J.
Human cytoplasmic serine hydroxymethyltransferase is an mRNA binding protein
Biochemistry
39
11523-11531
2000
Homo sapiens
Manually annotated by BRENDA team
Lewis, R.M.; Godfrey, K.M.; Jackson, A.A.; Cameron, I.T.; Hanson, M.A.
Low serine hydroxymethyltransferase activity in the human placenta has important implications for fetal glycine supply
J. Clin. Endocrinol. Metab.
90
1594-1598
2005
Ovis aries, Homo sapiens, Rattus norvegicus
Manually annotated by BRENDA team
Agrawal, S.; Kumar, A.; Srivastava, V.; Mishra, B.N.
Cloning, expression, activity and folding studies of serine hydroxymethyltransferase: a target enzyme for cancer chemotherapy
J. Mol. Microbiol. Biotechnol.
6
67-75
2003
Escherichia coli, Homo sapiens
Manually annotated by BRENDA team
Fu, T.F.; Hunt, S.; Schirch, V.; Safo, M.K.; Chen, B.H.
Properties of human and rabbit cytosolic serine hydroxymethyltransferase are changed by single nucleotide polymorphic mutations
Arch. Biochem. Biophys.
442
92-101
2005
Homo sapiens, Oryctolagus cuniculus (P07511), Oryctolagus cuniculus
Manually annotated by BRENDA team
Perry, C.; Sastry, R.; Nasrallah, I.M.; Stover, P.J.
Mimosine attenuates serine hydroxymethyltransferase transcription by chelating zinc: implications for inhibition of DNA replication
J. Biol. Chem.
280
396-400
2005
Homo sapiens
Manually annotated by BRENDA team
Franca, T.C.; Wilter, A.; Ramalho, T.C.; Pascutti, P.G.; Figueroa-Villar, J.D.
Molecular dynamics of the interaction of Plasmodium falciparum and human serine hydroxymethyltransferase with 5-formyl-6-hydrofolic acid analogues: design of new potential antimalarials
J. Braz. Chem. Soc.
17
1383-1392
2006
Plasmodium falciparum, Homo sapiens (P34896)
-
Manually annotated by BRENDA team
Choi, M.
Human serine hydroxymethyltransferase 2 (SHMT2) interacts with hnRNP D
Genes Genomics
30
541-548
2008
Homo sapiens
-
Manually annotated by BRENDA team
Siglioccolo, A.; Bossa, F.; Pascarella, S.
Structural adaptation of serine hydroxymethyltransferase to low temperatures
Int. J. Biol. Macromol.
46
37-46
2010
Geobacillus stearothermophilus, Oryctolagus cuniculus, Escherichia coli, Homo sapiens, Mus musculus
Manually annotated by BRENDA team
Fox, J.T.; Stover, P.J.
Mechanism of the internal ribosome entry site-mediated translation of serine hydroxymethyltransferase 1
J. Biol. Chem.
284
31085-31096
2009
Homo sapiens
Manually annotated by BRENDA team
Fox, J.T.; Shin, W.K.; Caudill, M.A.; Stover, P.J.
A UV-responsive internal ribosome entry site enhances serine hydroxymethyltransferase 1 expression for DNA damage repair
J. Biol. Chem.
284
31097-31108
2009
Homo sapiens
Manually annotated by BRENDA team
Anderson, D.D.; Woeller, C.F.; Chiang, E.P.; Shane, B.; Stover, P.J.
Serine hydroxymethyltransferase anchors de novo thymidylate synthesis pathway to nuclear lamina for DNA synthesis
J. Biol. Chem.
287
7051-7062
2012
Homo sapiens
Manually annotated by BRENDA team
Pinthong, C.; Maenpuen, S.; Amornwatcharapong, W.; Yuthavong, Y.; Leartsakulpanich, U.; Chaiyen, P.
Distinct biochemical properties of human serine hydroxymethyltransferase compared with the Plasmodium enzyme: implications for selective inhibition
FEBS J.
281
2570-2583
2014
Plasmodium falciparum, Plasmodium vivax, Homo sapiens (P34896), Homo sapiens
Manually annotated by BRENDA team
di Salvo, M.L.; Contestabile, R.; Paiardini, A.; Maras, B.
Glycine consumption and mitochondrial serine hydroxymethyltransferase in cancer cells: the heme connection
Med. Hypotheses
80
633-636
2013
Homo sapiens (P34897)
Manually annotated by BRENDA team
Kim, D.; Fiske, B.P.; Birsoy, K.; Freinkman, E.; Kami, K.; Possemato, R.L.; Chudnovsky, Y.; Pacold, M.E.; Chen, W.W.; Cantor, J.R.; Shelton, L.M.; Gui, D.Y.; Kwon, M.; Ramkissoon, S.H.; Ligon, K.L.; Kang, S.W.; Snuderl, M.; Vander Heiden, M.G.; Sabatini, D.M.
SHMT2 drives glioma cell survival in ischaemia but imposes a dependence on glycine clearance
Nature
520
363-367
2015
Homo sapiens (P34897), Homo sapiens
Manually annotated by BRENDA team
Yin, K.
Positive correlation between expression level of mitochondrial serine hydroxymethyltransferase and breast cancer grade
OncoTargets Ther.
8
1069-1074
2015
Homo sapiens
Manually annotated by BRENDA team
Amornwatcharapong, W.; Maenpuen, S.; Chitnumsub, P.; Leartsakulpanich, U.; Chaiyen, P.
Human and Plasmodium serine hydroxymethyltransferases differ in rate-limiting steps and pH-dependent substrate inhibition behavior
Arch. Biochem. Biophys.
630
91-100
2017
Homo sapiens, Plasmodium vivax
Manually annotated by BRENDA team
Tramonti, A.; Nardella, C.; di Salvo, M.L.; Barile, A.; Cutruzzola, F.; Contestabile, R.
Human cytosolic and mitochondrial serine hydroxymethyltransferase isoforms in comparison full kinetic characterization and substrate inhibition properties
Biochemistry
57
6984-6996
2018
Homo sapiens (P34896), Homo sapiens (P34897), Homo sapiens
Manually annotated by BRENDA team
Paiardini, A.; Tramonti, A.; Schirch, D.; Guiducci, G.; di Salvo, M.L.; Fiascarelli, A.; Giorgi, A.; Maras, B.; Cutruzzola, F.; Contestabile, R.
Differential 3-bromopyruvate inhibition of cytosolic and mitochondrial human serine hydroxymethyltransferase isoforms, key enzymes in cancer metabolic reprogramming
Biochim. Biophys. Acta
1864
1506-1517
2016
Homo sapiens (P34896), Homo sapiens (P34897), Homo sapiens
Manually annotated by BRENDA team
Paiardini, A.; Fiascarelli, A.; Rinaldo, S.; Daidone, F.; Giardina, G.; Koes, D.R.; Parroni, A.; Montini, G.; Marani, M.; Paone, A.; McDermott, L.A.; Contestabile, R.; Cutruzzola, F.
Screening and in vitro testing of antifolate inhibitors of human cytosolic serine hydroxymethyltransferase
ChemMedChem
10
490-497
2015
Homo sapiens
Manually annotated by BRENDA team
Giardina, G.; Brunotti, P.; Fiascarelli, A.; Cicalini, A.; Costa, M.G.; Buckle, A.M.; di Salvo, M.L.; Giorgi, A.; Marani, M.; Paone, A.; Rinaldo, S.; Paiardini, A.; Contestabile, R.; Cutruzzola, F.
How pyridoxal 5'-phosphate differentially regulates human cytosolic and mitochondrial serine hydroxymethyltransferase oligomeric state
FEBS J.
282
1225-1241
2015
Homo sapiens (P34896), Homo sapiens (P34897), Homo sapiens
Manually annotated by BRENDA team
Giardina, G.; Paone, A.; Tramonti, A.; Lucchi, R.; Marani, M.; Magnifico, M.C.; Bouzidi, A.; Pontecorvi, V.; Guiducci, G.; Zamparelli, C.; Rinaldo, S.; Paiardini, A.; Contestabile, R.; Cutruzzola, F.
The catalytic activity of serine hydroxymethyltransferase is essential for de novo nuclear dTMP synthesis in lung cancer cells
FEBS J.
285
3238-3253
2018
Homo sapiens (P34896)
Manually annotated by BRENDA team
Scaletti, E.; Jemth, A.S.; Helleday, T.; Stenmark, P.
Structural basis of inhibition of the human serine hydroxymethyltransferase SHMT2 by antifolate drugs
FEBS Lett.
593
1863-1873
2019
Homo sapiens (P34897), Homo sapiens
Manually annotated by BRENDA team