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Information on EC 2.1.2.1 - glycine hydroxymethyltransferase and Organism(s) Escherichia coli and UniProt Accession P0A825
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2.1.2.1 glycine hydroxymethyltransferaseIUBMB Comments
A pyridoxal-phosphate protein. Also catalyses the reaction of glycine with acetaldehyde to form L-threonine, and with 4-trimethylammoniobutanal to form 3-hydroxy-N6,N6,N6-trimethyl-L-lysine.
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Word Map
- 2.1.2.1
-
one-carbon
- pyridoxal
- thymidylate
- purine
- 5'-phosphate
- homocysteine
- dihydrofolate
-
folate-dependent
-
photorespiratory
-
photorespiration
-
folate-mediated
- pyridoxal-5'-phosphate
- thf
- dtmp
- mthfd1
-
plp-dependent
-
remethylation
-
aldimine
- phgdh
- medicine
-
folate-metabolizing
- 5,10-methenyltetrahydrofolate
-
5'-phosphate-dependent
- antifolate
- hydroxypyruvate
-
quinonoid
- 5-methyltetrahydrofolate
- glycerate
- 5-formyltetrahydrofolate
- drug development
-
folate-related
- d-alanine
-
c1-tetrahydrofolate
-
1-carbon
-
5-formyl
- polyglutamate
- l-threonine
-
alpha-protons
-
slc19a1
-
retro-aldol
- degradation
- analysis
- synthesis
- biotechnology
- pharmacology
The taxonomic range for the selected organisms is: Escherichia coli
The enzyme appears in selected viruses and cellular organisms
The enzyme appears in selected viruses and cellular organisms
Synonyms
serine hydroxymethyltransferase, shmt2, shmt1, serine hydroxymethyl transferase, serine transhydroxymethylase, serine hydroxymethyltransferase 2, mitochondrial serine hydroxymethyltransferase, serine hydroxymethyltransferase 1, bsshmt, pvshmt, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
L-serine hydroxymethyltransferase
-
-
-
-
serine hydroxymethylase hydroxymethyltransferase, serine
-
-
-
-
serine hydroxymethyltransferase
serine transhydroxymethylase
-
-
-
-
serine hydroxymethyltransferase
-
-
-
-
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
5,10-methylenetetrahydrofolate + glycine + H2O = tetrahydrofolate + L-serine
mechanism
5,10-methylenetetrahydrofolate + glycine + H2O = tetrahydrofolate + L-serine
mechanism
-
5,10-methylenetetrahydrofolate + glycine + H2O = tetrahydrofolate + L-serine
enzyme exhibits threonine aldolase activity (EC 4.1.2.5), but the two enzymes are distinct
-
5,10-methylenetetrahydrofolate + glycine + H2O = tetrahydrofolate + L-serine
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
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydroxymethyl group transfer
-
-
-
-
PATHWAY SOURCE
PATHWAYS
KEGG
-
-, -, -, -, -, -, -, -, -, -, -, -, -, -
SYSTEMATIC NAME
IUBMB Comments
5,10-methylenetetrahydrofolate:glycine hydroxymethyltransferase
A pyridoxal-phosphate protein. Also catalyses the reaction of glycine with acetaldehyde to form L-threonine, and with 4-trimethylammoniobutanal to form 3-hydroxy-N6,N6,N6-trimethyl-L-lysine.
CAS REGISTRY NUMBER
COMMENTARY
9029-83-8
-
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
5,10-methylenetetrahydrofolate + glycine + H2O
tetrahydrofolate + L-serine
-
-
-
r
tetrahydrofolate + L-serine
5,10-methylenetetrahydrofolate + glycine + H2O
-
-
-
r
alpha-methylserine + tetrahydrofolate
D-alanine + 5,10-methylenetetrahydrofolate
-
-
-
-
?
L-serine + tetrahydropteroylglutamate
glycine + 5,10-methylene-tetrahydropteroylglutamate + H2O
-
-
-
-
r
L-serine + tetrahydrofolate
glycine + 5,10-methylenetetrahydrofolate + H2O
-
-
-
?
L-serine + tetrahydrofolate
glycine + 5,10-methylenetetrahydrofolate + H2O
-
-
-
-
?
L-serine + tetrahydrofolate
glycine + 5,10-methylenetetrahydrofolate + H2O
-
-
-
r
L-serine + tetrahydrofolate
glycine + 5,10-methylenetetrahydrofolate + H2O
-
-
-
-
?
L-serine + tetrahydrofolate
glycine + 5,10-methylenetetrahydrofolate + H2O
-
-
-
?
L-serine + tetrahydrofolate
glycine + 5,10-methylenetetrahydrofolate + H2O
-
-
-
-
r
L-serine + tetrahydrofolate
glycine + 5,10-methylenetetrahydrofolate + H2O
-
-
-
r
L-serine + tetrahydrofolate
glycine + 5,10-methylenetetrahydrofolate + H2O
-
major pathway for production of C1-units of 5,10-methylenetetrahydrofolate
-
?
L-serine + tetrahydrofolate
glycine + 5,10-methylenetetrahydrofolate + H2O
-
major pathway for production of C1-units of 5,10-methylenetetrahydrofolate
-
?
L-serine + tetrahydrofolate
glycine + 5,10-methylenetetrahydrofolate + H2O
-
catalyzes interconversion of serine and glycine
-
?
L-serine + tetrahydrofolate
glycine + 5,10-methylenetetrahydrofolate + H2O
-
enzyme plays a pivotal role in channelling metabolites between amino acid and nucleotide metabolism
-
?
additional information
?
-
enzyme catalyzes the pyridoxal 5'-phosphate dependent reversible cleavage of 3-hydroxy-alpha-amino acids
-
-
?
additional information
?
-
-
enzyme catalyzes the pyridoxal 5'-phosphate dependent reversible cleavage of 3-hydroxy-alpha-amino acids
-
-
?
additional information
?
-
enzyme transaminates D-alanine to pyruvate and pyridoxamine phosphate
-
-
?
additional information
?
-
-
enzyme transaminates D-alanine to pyruvate and pyridoxamine phosphate
-
-
?
additional information
?
-
enzyme catalyses the racemization of D- and L-alanine
-
-
?
additional information
?
-
-
enzyme catalyses the racemization of D- and L-alanine
-
-
?
additional information
?
-
-
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
?
-
-
SHMT also catalyzes the hydrolysis of 5,10-methenyl-tetrahydropteroylglutamate to 5-formyl-tetrahydropteroylglutamate
-
-
?
additional information
?
-
-
broad substrate and reaction specificity, overview
-
-
?
additional information
?
-
-
SHMT activity with beta-phenylserine as substrate is about 1.48fold and 1.25fold higher than that with beta-(methylsulfonylphenyl) serine and beta-(nitrophenyl) serine as substrate, respectively. Besides SHMT activity, the enzyme also shows L-allo-threonine aldolase activity, EC 4.1.2.48
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
5,10-methylenetetrahydrofolate + glycine + H2O
tetrahydrofolate + L-serine
-
-
-
r
tetrahydrofolate + L-serine
5,10-methylenetetrahydrofolate + glycine + H2O
-
-
-
r
L-serine + tetrahydropteroylglutamate
glycine + 5,10-methylene-tetrahydropteroylglutamate + H2O
-
-
-
-
r
additional information
?
-
-
SHMT also catalyzes the hydrolysis of 5,10-methenyl-tetrahydropteroylglutamate to 5-formyl-tetrahydropteroylglutamate
-
-
?
L-serine + tetrahydrofolate
glycine + 5,10-methylenetetrahydrofolate + H2O
-
major pathway for production of C1-units of 5,10-methylenetetrahydrofolate
-
?
L-serine + tetrahydrofolate
glycine + 5,10-methylenetetrahydrofolate + H2O
-
major pathway for production of C1-units of 5,10-methylenetetrahydrofolate
-
?
L-serine + tetrahydrofolate
glycine + 5,10-methylenetetrahydrofolate + H2O
-
catalyzes interconversion of serine and glycine
-
?
L-serine + tetrahydrofolate
glycine + 5,10-methylenetetrahydrofolate + H2O
-
enzyme plays a pivotal role in channelling metabolites between amino acid and nucleotide metabolism
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
tetrahydrofolate
-
requirement with L-serine or L-2-methylserine as substrate
pyridoxal 5'-phosphate
-
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
pyridoxal 5'-phosphate
-
dependent on, stabilizes the dimeric form of the enzyme
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
D-alanine
inactivates enzyme by converting the enzyme bound pyridoxal 5'-phosphate to pyridoxamine phosphate in a transamination reaction
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
D-alanine
-
inactivates enzyme by converting the enzyme bound pyridoxal 5'-phosphate to pyridoxamine phosphate in a transamination reaction
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.14
L-serine
apparent value, wild type enzyme, at 20°C in 50 mM Na-HEPES (pH 7.2), containing 0.2 mM dithiothreitol and 0.1 mM EDTA
0.15
L-serine
apparent value, mutant enzyme L85A, at 20°C in 50 mM Na-HEPES (pH 7.2), containing 0.2 mM dithiothreitol and 0.1 mM EDTA
0.2
L-serine
apparent value, mutant enzyme L276A, at 20°C in 50 mM Na-HEPES (pH 7.2), containing 0.2 mM dithiothreitol and 0.1 mM EDTA
0.2
L-serine
apparent value, mutant enzyme L85A/L276A, at 20°C in 50 mM Na-HEPES (pH 7.2), containing 0.2 mM dithiothreitol and 0.1 mM EDTA
0.00435
tetrahydrofolate
apparent value, mutant enzyme L276A, at 20°C 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 20°C 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 20°C in 50 mM Na-HEPES (pH 7.2), containing 0.2 mM dithiothreitol and 0.1 mM EDTA
0.0112
tetrahydrofolate
apparent value, mutant enzyme L85A/L276A, at 20°C in 50 mM Na-HEPES (pH 7.2), containing 0.2 mM dithiothreitol and 0.1 mM EDTA
0.3
L-serine
-
wild-type enzyme, pH and temperature not specified in the publication
additional information
additional information
steady-state kinetics
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
6.7
L-serine
mutant enzyme L276A, at 20°C in 50 mM Na-HEPES (pH 7.2), containing 0.2 mM dithiothreitol and 0.1 mM EDTA
6.7
L-serine
mutant enzyme L85A/L276A, at 20°C in 50 mM Na-HEPES (pH 7.2), containing 0.2 mM dithiothreitol and 0.1 mM EDTA
10.8
L-serine
mutant enzyme L85A, at 20°C 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 20°C in 50 mM Na-HEPES (pH 7.2), containing 0.2 mM dithiothreitol and 0.1 mM EDTA
640
L-serine
-
wild-type enzyme, pH and temperature not specified in the publication
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
35.5
L-serine
-
wild-type enzyme, pH and temperature not specified in the publication
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
-
maximal activity of 6.3 U/mg total protein is reached
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
SHMT is a ubiquitous enzyme and its sequence and structure were conserved during divergent evolution. SHMT belongs to the fold type-I superfamily of PLP-dependent enzymes, a very complex group of proteins arising from an intricate evolutionary process
physiological function
SHMTs are an important group of pyridoxal-5'-phosphate-dependent enzymes that catalyze the reversible conversion of L-serine and tetrahydropteroylglutamate to glycine and 5,10-methylenetetrahydropteroylglutamate. The enzyme plays a central role in one-carbon unit metabolism. SHMT also catalyzes the 5,10-methylenetetrahydropteroylglutamate-independent cleavage of many 3-hydroxyamino acids and the decarboxylation of aminomalonate, at rates similar to that of H4PteGlu-dependent serine cleavage
evolution
-
serine hydroxymethyltransferase is a ubiquitous representative of the family of fold type I pyridoxal 5'-phosphate-dependent enzymes, structural determinants, 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
-
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
additional information
analysis of buried water clusters in the inner region of the SHMT dimers using the enzyme crystal structure, PDB 1DFO, molecular dynamics, overview
PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
91000
91000
wild type SHMT exists as a dimer in both apo- and holo-forms, ultracentrifugation
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
monomer
the apo-L276A and the apo-L85A mutants are in the monomeric state
dimer
homotetramer
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
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
analysis of buried water clusters in the inner region of the SHMT dimers using the enzyme crystal structure, molecular dynamics, overview
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
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
L276A
L785A/L276A
the mutation has the effect of lowering the cooperativity of urea denaturation process
L85A
L85A/L276A
the mutant is in the monomeric state and shows reduced activity
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
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
-
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
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 3.5°C lower than the wild-type Tm-value. The Tm-value in presence of Ser is 4°C 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 3.5°C higher than the wild-type Tm-value, The Tm-value in presence of Ser is 0.5°C 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
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 9°C lower than the wild-type Tm-value. The Tm-value in presence of Ser is 11.5°C lower than the wild-type value
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
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
L85A
the apo-L85A mutant enzyme is approximately 75% dimeric and shows reduced activity
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
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
60
-
for 10 min, the native enzyme conserves about 40% of its activity, while the mutant 3E7 retains about 56% of its activity
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
DEAE-Sepharose column chromatography and Phenyl-Sepharose column chromatography
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
Escherichia coli DH5alpha-PUC19 and Escherichia coli BL21 (DE3) used as host-vector system
-
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
-
RENATURED/Commentary
ORGANISM
UNIPROT
LITERATURE
denatured SHMT samples (0.023 mM in 8 M urea at 20°C) 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 20°C
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
drug development
the enzyme represents a potential target for chemotherapeutics
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
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 45°C. The immobilized cells are continuously used 10 times, yielding an average conversion rate of 60.4%
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Schirch, V.; Hopkins, S.; Villar, E.; Angelaccio, S.
Serine hydroxymethyltransferase from Escherichia coli: purification and properties
J. Bacteriol.
163
1-7
1985
Escherichia coli
Stover, P.; Schirch, V.
5-Formyltetrahydrofolate polyglutamates are slow tight binding inhibitors of serine hydroxymethyltransferase
J. Biol. Chem.
266
1543-1550
1991
Oryctolagus cuniculus, Escherichia coli
Contestabile, R.; Paiardini, A.; Pascarella, S.; Di Salvo, M.L.; D'Aguanno, S.; Bossa, F.
L-Threonine aldolase, serine hydroxymethyltransferase and fungal alanine racemase. A subgroup of strictly related enzymes specialized for different functions
Eur. J. Biochem.
268
6508-6525
2001
Escherichia coli (P0A825), Escherichia coli
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
Liu, J.Q.; Ito, S.; Dairi, T.; Itoh, N.; Kataoka, M.; Shimizu, S.; Yamada, H.
Gene cloning, nucleotide sequencing, and purification and characterization of the low-specificity L-threonine aldolase from Pseudomonas sp. strain NCIMB 10558
Appl. Environ. Microbiol.
64
549-554
1998
Escherichia coli
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
Fu, T.F.; Boja, E.S.; Safo, M.K.; Schirch, V.
Role of proline residues in the folding of serine hydroxymethyltransferase
J. Biol. Chem.
278
31088-31094
2003
Escherichia coli
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
Zuo, Z.; Zheng, Z.; Liu, Z.; Yi, Q.; Zou, G.
Cloning, DNA shuffling and expression of serine hydroxymethyltransferase gene from Escherichia coli strain AB90054
Enzyme Microb. Technol.
40
569-577
2007
Escherichia coli, Escherichia coli AB90054
-
Makart Stefa, M.S.; Heinemann Matthia, H.M.; Panke Sve, P.S.
Characterization of the AlkS/P(alkB)-expression system as an efficient tool for the production of recombinant proteins in Escherichia coli fed-batch fermentations
Biotechnol. Bioeng.
96
326-336
2007
Escherichia coli
Florio, R.; Chiaraluce, R.; Consalvi, V.; Paiardini, A.; Catacchio, B.; Bossa, F.; Contestabile, R.
The role of evolutionarily conserved hydrophobic contacts in the quaternary structure stability of Escherichia coli serine hydroxymethyltransferase
FEBS J.
276
132-143
2009
Escherichia coli (P0A825), Escherichia coli
Florio, R.; Chiaraluce, R.; Consalvi, V.; Paiardini, A.; Catacchio, B.; Bossa, F.; Contestabile, R.
Structural stability of the cofactor binding site in Escherichia coli serine hydroxymethyltransferase - the role of evolutionarily conserved hydrophobic contacts
FEBS J.
276
7319-7328
2009
Escherichia coli (P0A825), Escherichia coli
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
Zhao, G.H.; Li, H.; Liu, W.; Zhang, W.G.; Zhang, F.; Liu, Q.; Jiao, Q.C.
Preparation of optically active beta-hydroxy-alpha-amino acid by immobilized Escherichia coli cells with serine hydroxymethyl transferase activity
Amino Acids
40
215-220
2011
Escherichia coli, Escherichia coli K-12 MG1655
Florio, R.; di Salvo, M.L.; Vivoli, M.; Contestabile, R.
Serine hydroxymethyltransferase: a model enzyme for mechanistic, structural, and evolutionary studies
Biochim. Biophys. Acta
1814
1489-1496
2011
Bacillus subtilis, Escherichia coli
Angelaccio, S.; Di Salvo, M.; Parroni, A.; Di Bello, A.; Contestabile, R.; Pascarella, S.
Structural stability of cold-adapted serine hydroxymethyltransferase, a tool for beta-hydroxy-alpha-amino acid biosynthesis
J. Mol. Catal. B
110
171-177
2014
Psychromonas ingrahamii (A1SUU0), Escherichia coli (P0A825), Psychromonas ingrahamii 37 (A1SUU0)
-
Milano, T.; Di Salvo, M.L.; Angelaccio, S.; Pascarella, S.
Conserved water molecules in bacterial serine hydroxymethyltransferases
Protein Eng. Des. Sel.
28
415-426
2015
Burkholderia pseudomallei (A0A069BAT4), Psychromonas ingrahamii (A1SUU0), Rickettsia rickettsii (A8GTI9), Burkholderia cenocepacia (B4ECY9), Salmonella enterica subsp. enterica serovar Typhimurium (P0A2E1), Escherichia coli (P0A825), Mycobacterium tuberculosis (P9WGI9), Staphylococcus aureus (Q5HE87), Thermus thermophilus (Q5SI56), Geobacillus stearothermophilus (Q7SIB6), Campylobacter jejuni (Q9S6K1), Campylobacter jejuni ATCC 33560 (Q9S6K1), Psychromonas ingrahamii 37 (A1SUU0), Mycobacterium tuberculosis H37Rv (P9WGI9), Staphylococcus aureus COL (Q5HE87), Burkholderia pseudomallei ATCC 23343 (A0A069BAT4), Rickettsia rickettsii Sheila Smith (A8GTI9)
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