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Literature summary extracted from

  • Milano, T.; Di Salvo, M.L.; Angelaccio, S.; Pascarella, S.
    Conserved water molecules in bacterial serine hydroxymethyltransferases (2015), Protein Eng. Des. Sel., 28, 415-426.
    View publication on PubMed

Application

EC Number Application Comment Organism
2.1.2.1 drug development the enzyme represents a potential target for chemotherapeutics Mycobacterium tuberculosis
2.1.2.1 drug development the enzyme represents a potential target for chemotherapeutics Escherichia coli
2.1.2.1 drug development the enzyme represents a potential target for chemotherapeutics Geobacillus stearothermophilus
2.1.2.1 drug development the enzyme represents a potential target for chemotherapeutics Psychromonas ingrahamii
2.1.2.1 drug development the enzyme represents a potential target for chemotherapeutics Staphylococcus aureus
2.1.2.1 drug development the enzyme represents a potential target for chemotherapeutics Thermus thermophilus
2.1.2.1 drug development the enzyme represents a potential target for chemotherapeutics Burkholderia pseudomallei
2.1.2.1 drug development the enzyme represents a potential target for chemotherapeutics Salmonella enterica subsp. enterica serovar Typhimurium
2.1.2.1 drug development the enzyme represents a potential target for chemotherapeutics Campylobacter jejuni
2.1.2.1 drug development the enzyme represents a potential target for chemotherapeutics Rickettsia rickettsii
2.1.2.1 drug development the enzyme represents a potential target for chemotherapeutics Burkholderia cenocepacia

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2.1.2.1 5,10-methylenetetrahydrofolate + glycine + H2O Mycobacterium tuberculosis
-
 tetrahydrofolate + L-serine
-
 r
2.1.2.1 5,10-methylenetetrahydrofolate + glycine + H2O Escherichia coli
-
 tetrahydrofolate + L-serine
-
 r
2.1.2.1 5,10-methylenetetrahydrofolate + glycine + H2O Geobacillus stearothermophilus
-
 tetrahydrofolate + L-serine
-
 r
2.1.2.1 5,10-methylenetetrahydrofolate + glycine + H2O Psychromonas ingrahamii
-
 tetrahydrofolate + L-serine
-
 r
2.1.2.1 5,10-methylenetetrahydrofolate + glycine + H2O Staphylococcus aureus
-
 tetrahydrofolate + L-serine
-
 r
2.1.2.1 5,10-methylenetetrahydrofolate + glycine + H2O Thermus thermophilus
-
 tetrahydrofolate + L-serine
-
 r
2.1.2.1 5,10-methylenetetrahydrofolate + glycine + H2O Burkholderia pseudomallei
-
 tetrahydrofolate + L-serine
-
 r
2.1.2.1 5,10-methylenetetrahydrofolate + glycine + H2O Salmonella enterica subsp. enterica serovar Typhimurium
-
 tetrahydrofolate + L-serine
-
 r
2.1.2.1 5,10-methylenetetrahydrofolate + glycine + H2O Campylobacter jejuni
-
 tetrahydrofolate + L-serine
-
 r
2.1.2.1 5,10-methylenetetrahydrofolate + glycine + H2O Rickettsia rickettsii
-
 tetrahydrofolate + L-serine
-
 r
2.1.2.1 5,10-methylenetetrahydrofolate + glycine + H2O Burkholderia cenocepacia
-
 tetrahydrofolate + L-serine
-
 r
2.1.2.1 5,10-methylenetetrahydrofolate + glycine + H2O Campylobacter jejuni ATCC 33560
-
 tetrahydrofolate + L-serine
-
 r
2.1.2.1 5,10-methylenetetrahydrofolate + glycine + H2O Psychromonas ingrahamii 37
-
 tetrahydrofolate + L-serine
-
 r
2.1.2.1 5,10-methylenetetrahydrofolate + glycine + H2O Mycobacterium tuberculosis H37Rv
-
 tetrahydrofolate + L-serine
-
 r
2.1.2.1 5,10-methylenetetrahydrofolate + glycine + H2O Staphylococcus aureus COL
-
 tetrahydrofolate + L-serine
-
 r
2.1.2.1 5,10-methylenetetrahydrofolate + glycine + H2O Burkholderia pseudomallei ATCC 23343
-
 tetrahydrofolate + L-serine
-
 r
2.1.2.1 5,10-methylenetetrahydrofolate + glycine + H2O Rickettsia rickettsii Sheila Smith
-
 tetrahydrofolate + L-serine
-
 r

Organism

EC Number Organism UniProt Comment Textmining
2.1.2.1 Burkholderia cenocepacia B4ECY9 gene glyA
-
2.1.2.1 Burkholderia pseudomallei A0A069BAT4 gene glyA
-
2.1.2.1 Burkholderia pseudomallei ATCC 23343 A0A069BAT4 gene glyA
-
2.1.2.1 Campylobacter jejuni Q9S6K1 gene glyA
-
2.1.2.1 Campylobacter jejuni ATCC 33560 Q9S6K1 gene glyA
-
2.1.2.1 Escherichia coli P0A825 gene glyA
-
2.1.2.1 Geobacillus stearothermophilus Q7SIB6 gene glyA
-
2.1.2.1 Mycobacterium tuberculosis P9WGI9 gene glyA1
-
2.1.2.1 Mycobacterium tuberculosis H37Rv P9WGI9 gene glyA1
-
2.1.2.1 Psychromonas ingrahamii A1SUU0 gene glyA
-
2.1.2.1 Psychromonas ingrahamii 37 A1SUU0 gene glyA
-
2.1.2.1 Rickettsia rickettsii A8GTI9 gene glyA
-
2.1.2.1 Rickettsia rickettsii Sheila Smith A8GTI9 gene glyA
-
2.1.2.1 Salmonella enterica subsp. enterica serovar Typhimurium P0A2E1 gene glyA
-
2.1.2.1 Staphylococcus aureus Q5HE87 gene glyA
-
2.1.2.1 Staphylococcus aureus COL Q5HE87 gene glyA
-
2.1.2.1 Thermus thermophilus Q5SI56 gene glyA
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.1.2.1 5,10-methylenetetrahydrofolate + glycine + H2O
-
 Mycobacterium tuberculosis tetrahydrofolate + L-serine
-
 r
2.1.2.1 5,10-methylenetetrahydrofolate + glycine + H2O
-
 Escherichia coli tetrahydrofolate + L-serine
-
 r
2.1.2.1 5,10-methylenetetrahydrofolate + glycine + H2O
-
 Geobacillus stearothermophilus tetrahydrofolate + L-serine
-
 r
2.1.2.1 5,10-methylenetetrahydrofolate + glycine + H2O
-
 Psychromonas ingrahamii tetrahydrofolate + L-serine
-
 r
2.1.2.1 5,10-methylenetetrahydrofolate + glycine + H2O
-
 Staphylococcus aureus tetrahydrofolate + L-serine
-
 r
2.1.2.1 5,10-methylenetetrahydrofolate + glycine + H2O
-
 Thermus thermophilus tetrahydrofolate + L-serine
-
 r
2.1.2.1 5,10-methylenetetrahydrofolate + glycine + H2O
-
 Burkholderia pseudomallei tetrahydrofolate + L-serine
-
 r
2.1.2.1 5,10-methylenetetrahydrofolate + glycine + H2O
-
 Salmonella enterica subsp. enterica serovar Typhimurium tetrahydrofolate + L-serine
-
 r
2.1.2.1 5,10-methylenetetrahydrofolate + glycine + H2O
-
 Campylobacter jejuni tetrahydrofolate + L-serine
-
 r
2.1.2.1 5,10-methylenetetrahydrofolate + glycine + H2O
-
 Rickettsia rickettsii tetrahydrofolate + L-serine
-
 r
2.1.2.1 5,10-methylenetetrahydrofolate + glycine + H2O
-
 Burkholderia cenocepacia tetrahydrofolate + L-serine
-
 r
2.1.2.1 5,10-methylenetetrahydrofolate + glycine + H2O
-
 Campylobacter jejuni ATCC 33560 tetrahydrofolate + L-serine
-
 r
2.1.2.1 5,10-methylenetetrahydrofolate + glycine + H2O
-
 Psychromonas ingrahamii 37 tetrahydrofolate + L-serine
-
 r
2.1.2.1 5,10-methylenetetrahydrofolate + glycine + H2O
-
 Mycobacterium tuberculosis H37Rv tetrahydrofolate + L-serine
-
 r
2.1.2.1 5,10-methylenetetrahydrofolate + glycine + H2O
-
 Staphylococcus aureus COL tetrahydrofolate + L-serine
-
 r
2.1.2.1 5,10-methylenetetrahydrofolate + glycine + H2O
-
 Burkholderia pseudomallei ATCC 23343 tetrahydrofolate + L-serine
-
 r
2.1.2.1 5,10-methylenetetrahydrofolate + glycine + H2O
-
 Rickettsia rickettsii Sheila Smith tetrahydrofolate + L-serine
-
 r

Subunits

EC Number Subunits Comment Organism
2.1.2.1 dimer analysis of buried water clusters in the inner region of the SHMT dimers using the enzyme crystal structure, molecular dynamics, overview Mycobacterium tuberculosis
2.1.2.1 dimer analysis of buried water clusters in the inner region of the SHMT dimers using the enzyme crystal structure, molecular dynamics, overview Escherichia coli
2.1.2.1 dimer analysis of buried water clusters in the inner region of the SHMT dimers using the enzyme crystal structure, molecular dynamics, overview Geobacillus stearothermophilus
2.1.2.1 dimer analysis of buried water clusters in the inner region of the SHMT dimers using the enzyme crystal structure, molecular dynamics, overview Psychromonas ingrahamii
2.1.2.1 dimer analysis of buried water clusters in the inner region of the SHMT dimers using the enzyme crystal structure, molecular dynamics, overview Staphylococcus aureus
2.1.2.1 dimer analysis of buried water clusters in the inner region of the SHMT dimers using the enzyme crystal structure, molecular dynamics, overview Thermus thermophilus
2.1.2.1 dimer analysis of buried water clusters in the inner region of the SHMT dimers using the enzyme crystal structure, molecular dynamics, overview Burkholderia pseudomallei
2.1.2.1 dimer analysis of buried water clusters in the inner region of the SHMT dimers using the enzyme crystal structure, molecular dynamics, overview Salmonella enterica subsp. enterica serovar Typhimurium
2.1.2.1 dimer analysis of buried water clusters in the inner region of the SHMT dimers using the enzyme crystal structure, molecular dynamics, overview Campylobacter jejuni
2.1.2.1 dimer analysis of buried water clusters in the inner region of the SHMT dimers using the enzyme crystal structure, molecular dynamics, overview Rickettsia rickettsii
2.1.2.1 dimer analysis of buried water clusters in the inner region of the SHMT dimers using the enzyme crystal structure, molecular dynamics, overview Burkholderia cenocepacia

Synonyms

EC Number Synonyms Comment Organism
2.1.2.1 serine hydroxymethyltransferase
-
 Mycobacterium tuberculosis
2.1.2.1 serine hydroxymethyltransferase
-
 Escherichia coli
2.1.2.1 serine hydroxymethyltransferase
-
 Geobacillus stearothermophilus
2.1.2.1 serine hydroxymethyltransferase
-
 Psychromonas ingrahamii
2.1.2.1 serine hydroxymethyltransferase
-
 Staphylococcus aureus
2.1.2.1 serine hydroxymethyltransferase
-
 Thermus thermophilus
2.1.2.1 serine hydroxymethyltransferase
-
 Burkholderia pseudomallei
2.1.2.1 serine hydroxymethyltransferase
-
 Salmonella enterica subsp. enterica serovar Typhimurium
2.1.2.1 serine hydroxymethyltransferase
-
 Campylobacter jejuni
2.1.2.1 serine hydroxymethyltransferase
-
 Rickettsia rickettsii
2.1.2.1 serine hydroxymethyltransferase
-
 Burkholderia cenocepacia
2.1.2.1 SHMT
-
 Mycobacterium tuberculosis
2.1.2.1 SHMT
-
 Escherichia coli
2.1.2.1 SHMT
-
 Geobacillus stearothermophilus
2.1.2.1 SHMT
-
 Psychromonas ingrahamii
2.1.2.1 SHMT
-
 Staphylococcus aureus
2.1.2.1 SHMT
-
 Thermus thermophilus
2.1.2.1 SHMT
-
 Burkholderia pseudomallei
2.1.2.1 SHMT
-
 Salmonella enterica subsp. enterica serovar Typhimurium
2.1.2.1 SHMT
-
 Campylobacter jejuni
2.1.2.1 SHMT
-
 Rickettsia rickettsii
2.1.2.1 SHMT
-
 Burkholderia cenocepacia

Cofactor

EC Number Cofactor Comment Organism Structure
2.1.2.1 5,10-methylenetetrahydrofolate
-
 Mycobacterium tuberculosis
2.1.2.1 5,10-methylenetetrahydrofolate
-
 Escherichia coli
2.1.2.1 5,10-methylenetetrahydrofolate
-
 Geobacillus stearothermophilus
2.1.2.1 5,10-methylenetetrahydrofolate
-
 Psychromonas ingrahamii
2.1.2.1 5,10-methylenetetrahydrofolate
-
 Staphylococcus aureus
2.1.2.1 5,10-methylenetetrahydrofolate
-
 Thermus thermophilus
2.1.2.1 5,10-methylenetetrahydrofolate
-
 Burkholderia pseudomallei
2.1.2.1 5,10-methylenetetrahydrofolate
-
 Salmonella enterica subsp. enterica serovar Typhimurium
2.1.2.1 5,10-methylenetetrahydrofolate
-
 Campylobacter jejuni
2.1.2.1 5,10-methylenetetrahydrofolate
-
 Rickettsia rickettsii
2.1.2.1 5,10-methylenetetrahydrofolate
-
 Burkholderia cenocepacia
2.1.2.1 pyridoxal 5'-phosphate dependent on Mycobacterium tuberculosis
2.1.2.1 pyridoxal 5'-phosphate dependent on Escherichia coli
2.1.2.1 pyridoxal 5'-phosphate dependent on Geobacillus stearothermophilus
2.1.2.1 pyridoxal 5'-phosphate dependent on Psychromonas ingrahamii
2.1.2.1 pyridoxal 5'-phosphate dependent on Staphylococcus aureus
2.1.2.1 pyridoxal 5'-phosphate dependent on Thermus thermophilus
2.1.2.1 pyridoxal 5'-phosphate dependent on Burkholderia pseudomallei
2.1.2.1 pyridoxal 5'-phosphate dependent on Salmonella enterica subsp. enterica serovar Typhimurium
2.1.2.1 pyridoxal 5'-phosphate dependent on Campylobacter jejuni
2.1.2.1 pyridoxal 5'-phosphate dependent on Rickettsia rickettsii
2.1.2.1 pyridoxal 5'-phosphate dependent on Burkholderia cenocepacia
2.1.2.1 tetrahydrofolate
-
 Mycobacterium tuberculosis
2.1.2.1 tetrahydrofolate
-
 Escherichia coli
2.1.2.1 tetrahydrofolate
-
 Geobacillus stearothermophilus
2.1.2.1 tetrahydrofolate
-
 Psychromonas ingrahamii
2.1.2.1 tetrahydrofolate
-
 Staphylococcus aureus
2.1.2.1 tetrahydrofolate
-
 Thermus thermophilus
2.1.2.1 tetrahydrofolate
-
 Burkholderia pseudomallei
2.1.2.1 tetrahydrofolate
-
 Salmonella enterica subsp. enterica serovar Typhimurium
2.1.2.1 tetrahydrofolate
-
 Campylobacter jejuni
2.1.2.1 tetrahydrofolate
-
 Rickettsia rickettsii
2.1.2.1 tetrahydrofolate
-
 Burkholderia cenocepacia

General Information

EC Number General Information Comment Organism
2.1.2.1 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 Mycobacterium tuberculosis
2.1.2.1 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 Escherichia coli
2.1.2.1 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 Geobacillus stearothermophilus
2.1.2.1 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 Psychromonas ingrahamii
2.1.2.1 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 Staphylococcus aureus
2.1.2.1 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 Thermus thermophilus
2.1.2.1 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 Burkholderia pseudomallei
2.1.2.1 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 Salmonella enterica subsp. enterica serovar Typhimurium
2.1.2.1 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 Campylobacter jejuni
2.1.2.1 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 Rickettsia rickettsii
2.1.2.1 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 Burkholderia cenocepacia
2.1.2.1 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 Escherichia coli
2.1.2.1 additional information analysis of buried water clusters in the inner region of the SHMT dimers using the enzyme crystal structure, PDB 1KKJ, molecular dynamics, overview Geobacillus stearothermophilus
2.1.2.1 additional information analysis of buried water clusters in the inner region of the SHMT dimers using the enzyme crystal structure, PDB 2DKJ, molecular dynamics, overview Thermus thermophilus
2.1.2.1 additional information analysis of buried water clusters in the inner region of the SHMT dimers using the enzyme crystal structure, PDB 3ECD, molecular dynamics, overview Burkholderia pseudomallei
2.1.2.1 additional information analysis of buried water clusters in the inner region of the SHMT dimers using the enzyme crystal structure, PDB 3GBX, molecular dynamics, overview Salmonella enterica subsp. enterica serovar Typhimurium
2.1.2.1 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 Mycobacterium tuberculosis
2.1.2.1 additional information analysis of buried water clusters in the inner region of the SHMT dimers using the enzyme crystal structure, PDB 3N0L, molecular dynamics, overview Campylobacter jejuni
2.1.2.1 additional information analysis of buried water clusters in the inner region of the SHMT dimers using the enzyme crystal structure, PDB 3PGY, molecular dynamics, overview Staphylococcus aureus
2.1.2.1 additional information analysis of buried water clusters in the inner region of the SHMT dimers using the enzyme crystal structure, PDB 4J5U, molecular dynamics, overview Rickettsia rickettsii
2.1.2.1 additional information analysis of buried water clusters in the inner region of the SHMT dimers using the enzyme crystal structure, PDB 4N0W, molecular dynamics, overview Burkholderia cenocepacia
2.1.2.1 additional information analysis of buried water clusters in the inner region of the SHMT dimers using the enzyme crystal structure, PDB 4P3M, molecular dynamics, overview Psychromonas ingrahamii
2.1.2.1 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 Escherichia coli
2.1.2.1 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 Mycobacterium tuberculosis
2.1.2.1 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 Geobacillus stearothermophilus
2.1.2.1 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 Psychromonas ingrahamii
2.1.2.1 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 Staphylococcus aureus
2.1.2.1 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 Thermus thermophilus
2.1.2.1 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 Burkholderia pseudomallei
2.1.2.1 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 Salmonella enterica subsp. enterica serovar Typhimurium
2.1.2.1 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 Campylobacter jejuni
2.1.2.1 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 Rickettsia rickettsii
2.1.2.1 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 Burkholderia cenocepacia