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Information on EC 2.1.2.1 - glycine hydroxymethyltransferase and Organism(s) Mycobacterium tuberculosis and UniProt Accession P9WGI7

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EC Tree
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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This record set is specific for:
Mycobacterium tuberculosis
UNIPROT: P9WGI7
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The taxonomic range for the selected organisms is: Mycobacterium tuberculosis
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
glycine hydroxymethyltransferrase
-
L-serine hydroxymethyltransferase
-
-
-
-
serine hydroxymethylase hydroxymethyltransferase, serine
-
-
-
-
serine hydroxymethyltransferase
serine transhydroxymethylase
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydroxymethyl group transfer
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-
-
-
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
tetrahydrofolate + L-Ser
5,10-methylenetetrahydrofolate + glycine
show the reaction diagram
-
-
-
r
5,10-methylenetetrahydrofolate + glycine + H2O
tetrahydrofolate + L-serine
show the reaction diagram
-
-
-
r
tetrahydrofolate + L-Ser
5,10-methylenetetrahydrofolate + glycine
show the reaction diagram
-
-
-
r
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
5,10-methylenetetrahydrofolate + glycine + H2O
tetrahydrofolate + L-serine
show the reaction diagram
-
-
-
r
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
pyridoxal 5'-phosphate
SHM2 contains 2 mol per mol of enzyme dimer
5,10-methylenetetrahydrofolate
-
pyridoxal 5'-phosphate
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
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 H4PteGlu-independent cleavage of many 3-hydroxyamino acids and the decarboxylation of aminomalonate, at rates similar to that of H4PteGlu-dependent serine cleavage
additional information
analysis of buried water clusters in the inner region of the SHMT dimers using the enzyme crystal structure, PDB 3H7F, molecular dynamics, overview
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
45500
2 * 45500, SHM2, SDS-PAGE
87100
SHM2, gel filtration
45000
2 * 45000, SHM1, SDS-PAGE
91200
SHM1, gel filtration
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dimer
2 * 45500, SHM2, SDS-PAGE
dimer
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
8
transition of SHM2 is between pH 6.5 and 11 and centered at about pH 8.0
659265
9
native SHM2 dimer dissociates into monomer
659265
10.5
resistant to alkaline denaturation up to, SHM1
659265
9.25
transition of SHM1 is between pH 8 and 11 and centered at about pH 9.25
659265
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
69
transition temperature of SHM1
60
transition temperature of SHM1
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
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
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
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
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
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
drug development
the enzyme represents a potential target for chemotherapeutics
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Chaturvedi, S.; Bhakuni, V.
Unusual structural, functional, and stability properties of serine hydroxymethyltransferase from Mycobacterium tuberculosis
J. Biol. Chem.
278
40793-40805
2003
Mycobacterium tuberculosis (P9WGI7), Mycobacterium tuberculosis (P9WGI9), Mycobacterium tuberculosis, Mycobacterium tuberculosis H37Rv (P9WGI7), Mycobacterium tuberculosis H37Rv (P9WGI9)
Manually annotated by BRENDA team
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)
Manually annotated by BRENDA team