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Literature summary for 2.6.1.45 extracted from

  • But, S.Y.; Egorova, S.V.; Khmelenina, V.N.; Trotsenko, Y.A.
    Serine-glyoxylate aminotranferases from methanotrophs using different C1-assimilation pathways (2019), Antonie van Leeuwenhoek, 112, 741-751 .
    View publication on PubMed
Search for more literature for 2.6.1.45

Cloned(Commentary)

Cloned (Comment) Organism
DNA and amino acid sequence determination and analysis, phylogenetic analysis, recombinant expression of His-tagged enzyme in Escherichia coli strain Rosetta (DE3) Methylosinus trichosporium
DNA and amino acid sequence determination and analysis, phylogenetic analysis, recombinant expression of His-tagged enzyme in Escherichia coli strain Rosetta (DE3) Methylotuvimicrobium alcaliphilum
DNA and amino acid sequence determination and analysis, phylogenetic analysis, recombinant expression of His-tagged enzyme in Escherichia coli strain Rosetta (DE3) Methylococcus capsulatus

Protein Variants

Protein Variants Comment Organism
additional information the sga20Z gene is knocked out by the insertion of the kanamycin cassette using double homologous recombination. The growth rate of the DELTAsga strain on methane is significantly lower as compared to the wild-type strain. During growth on methanol, this effect is even more pronounced Methylotuvimicrobium alcaliphilum

Inhibitors

Inhibitors Comment Organism Structure
2-oxoglutarate 2-oxoglutarate at a concentration above 12.5 mM inhibits enzyme SgaBath in the serine-2-oxoglutarate aminotransferase (SKAT) reaction, but has no effect on the serine-glyoxylate aminotranferase (SGAT) reaction, substrate inhibition Methylococcus capsulatus
2-oxoglutarate 2-oxoglutarate at a concentration above 12.5 mM inhibits enzyme Sga20Z in the serine-2-oxoglutarate aminotransferase (SKAT) reaction, but has no effect on the serine-glyoxylate aminotranferase (SGAT) reaction, substrate inhibition Methylotuvimicrobium alcaliphilum

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.089
-
 L-serine pH 7.5, temperature not specified in the publication, recombinant enzyme, with pyruvate Methylotuvimicrobium alcaliphilum
0.089
-
 L-serine pH 7.5, temperature not specified in the publication, recombinant enzyme, with pyruvate Methylococcus capsulatus
0.17
-
 glyoxylate pH 7.0, temperature not specified in the publication, recombinant enzyme, with L-serine Methylosinus trichosporium
0.18
-
 L-serine pH 7.0, temperature not specified in the publication, recombinant enzyme, with pyruvate Methylosinus trichosporium
0.24
-
 glyoxylate pH 7.5, temperature not specified in the publication, recombinant enzyme, with L-serine Methylotuvimicrobium alcaliphilum
0.59
-
 glyoxylate pH 7.5, temperature not specified in the publication, recombinant enzyme, with L-alanine Methylococcus capsulatus
0.7
-
 glyoxylate pH 7.5, temperature not specified in the publication, recombinant enzyme, with L-serine Methylococcus capsulatus
1
-
 glyoxylate pH 7.5, temperature not specified in the publication, recombinant enzyme, with L-alanine Methylotuvimicrobium alcaliphilum
1.06
-
 L-serine pH 7.5, temperature not specified in the publication, recombinant enzyme, with 2-oxoglutarate Methylococcus capsulatus
1.17
-
 L-serine pH 7.5, temperature not specified in the publication, recombinant enzyme, with 2-oxoglutarate Methylotuvimicrobium alcaliphilum
1.62
-
 L-serine pH 7.5, temperature not specified in the publication, recombinant enzyme, with glyoxylate Methylococcus capsulatus
2 3 L-alanine pH 7.5, temperature not specified in the publication, recombinant enzyme, with glyoxylate Methylococcus capsulatus
2.1
-
 L-serine pH 7.0, temperature not specified in the publication, recombinant enzyme, with glyoxylate Methylosinus trichosporium
2.6
-
 L-serine pH 7.5, temperature not specified in the publication, recombinant enzyme, with glyoxylate Methylotuvimicrobium alcaliphilum
4.3
-
 2-oxoglutarate pH 7.5, temperature not specified in the publication, recombinant enzyme, with L-serine Methylococcus capsulatus
4.5
-
 pyruvate pH 7.5, temperature not specified in the publication, recombinant enzyme, with L-serine Methylococcus capsulatus
5
-
 2-oxoglutarate pH 7.5, temperature not specified in the publication, recombinant enzyme, with L-serine Methylotuvimicrobium alcaliphilum
5.8
-
 pyruvate pH 7.0, temperature not specified in the publication, recombinant enzyme, with L-serine Methylosinus trichosporium
6
-
 pyruvate pH 7.5, temperature not specified in the publication, recombinant enzyme, with L-serine Methylotuvimicrobium alcaliphilum
14
-
 L-alanine pH 7.5, temperature not specified in the publication, recombinant enzyme, with glyoxylate Methylotuvimicrobium alcaliphilum

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
80000
-
 gel filtration Methylotuvimicrobium alcaliphilum
120000
-
 gel filtration Methylococcus capsulatus
170000
-
 gel filtration Methylosinus trichosporium

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
L-alanine + glyoxylate Methylotuvimicrobium alcaliphilum reaction of alanine-glyoxylate aminotransferase (AGAT), EC 2.6.1.44 pyruvate + glycine
-
 ?
L-alanine + glyoxylate Methylococcus capsulatus reaction of alanine-glyoxylate aminotransferase (AGAT), EC 2.6.1.44 pyruvate + glycine
-
 ?
L-alanine + glyoxylate Methylococcus capsulatus Bath reaction of alanine-glyoxylate aminotransferase (AGAT), EC 2.6.1.44 pyruvate + glycine
-
 ?
L-alanine + glyoxylate Methylotuvimicrobium alcaliphilum VKM B-2133 reaction of alanine-glyoxylate aminotransferase (AGAT), EC 2.6.1.44 pyruvate + glycine
-
 ?
L-alanine + glyoxylate Methylococcus capsulatus ATCC 33009 reaction of alanine-glyoxylate aminotransferase (AGAT), EC 2.6.1.44 pyruvate + glycine
-
 ?
L-alanine + glyoxylate Methylotuvimicrobium alcaliphilum 20Z reaction of alanine-glyoxylate aminotransferase (AGAT), EC 2.6.1.44 pyruvate + glycine
-
 ?
L-alanine + glyoxylate Methylococcus capsulatus NCIMB 11132 reaction of alanine-glyoxylate aminotransferase (AGAT), EC 2.6.1.44 pyruvate + glycine
-
 ?
L-alanine + glyoxylate Methylotuvimicrobium alcaliphilum DSM 19304 reaction of alanine-glyoxylate aminotransferase (AGAT), EC 2.6.1.44 pyruvate + glycine
-
 ?
L-alanine + glyoxylate Methylotuvimicrobium alcaliphilum NCIMB 14124 reaction of alanine-glyoxylate aminotransferase (AGAT), EC 2.6.1.44 pyruvate + glycine
-
 ?
L-serine + 2-oxoglutarate Methylotuvimicrobium alcaliphilum
-
 3-hydroxypyruvate + L-glutamate
-
 ?
L-serine + 2-oxoglutarate Methylococcus capsulatus
-
 3-hydroxypyruvate + L-glutamate
-
 ?
L-serine + 2-oxoglutarate Methylococcus capsulatus Bath
-
 3-hydroxypyruvate + L-glutamate
-
 ?
L-serine + 2-oxoglutarate Methylotuvimicrobium alcaliphilum VKM B-2133
-
 3-hydroxypyruvate + L-glutamate
-
 ?
L-serine + 2-oxoglutarate Methylococcus capsulatus ATCC 33009
-
 3-hydroxypyruvate + L-glutamate
-
 ?
L-serine + 2-oxoglutarate Methylotuvimicrobium alcaliphilum 20Z
-
 3-hydroxypyruvate + L-glutamate
-
 ?
L-serine + 2-oxoglutarate Methylococcus capsulatus NCIMB 11132
-
 3-hydroxypyruvate + L-glutamate
-
 ?
L-serine + 2-oxoglutarate Methylotuvimicrobium alcaliphilum DSM 19304
-
 3-hydroxypyruvate + L-glutamate
-
 ?
L-serine + 2-oxoglutarate Methylotuvimicrobium alcaliphilum NCIMB 14124
-
 3-hydroxypyruvate + L-glutamate
-
 ?
L-serine + glyoxylate Methylosinus trichosporium preferred substrates 3-hydroxypyruvate + glycine
-
 ?
L-serine + glyoxylate Methylotuvimicrobium alcaliphilum preferred substrates 3-hydroxypyruvate + glycine
-
 ?
L-serine + glyoxylate Methylococcus capsulatus preferred substrates 3-hydroxypyruvate + glycine
-
 ?
L-serine + glyoxylate Methylococcus capsulatus Bath preferred substrates 3-hydroxypyruvate + glycine
-
 ?
L-serine + glyoxylate Methylotuvimicrobium alcaliphilum VKM B-2133 preferred substrates 3-hydroxypyruvate + glycine
-
 ?
L-serine + glyoxylate Methylococcus capsulatus ATCC 33009 preferred substrates 3-hydroxypyruvate + glycine
-
 ?
L-serine + glyoxylate Methylotuvimicrobium alcaliphilum 20Z preferred substrates 3-hydroxypyruvate + glycine
-
 ?
L-serine + glyoxylate Methylococcus capsulatus NCIMB 11132 preferred substrates 3-hydroxypyruvate + glycine
-
 ?
L-serine + glyoxylate Methylotuvimicrobium alcaliphilum DSM 19304 preferred substrates 3-hydroxypyruvate + glycine
-
 ?
L-serine + glyoxylate Methylotuvimicrobium alcaliphilum NCIMB 14124 preferred substrates 3-hydroxypyruvate + glycine
-
 ?
L-serine + pyruvate Methylosinus trichosporium reaction of serine-pyruvate aminotransferase (SPAT), EC 2.6.1.51 3-hydroxypyruvate + L-alanine
-
 ?
L-serine + pyruvate Methylotuvimicrobium alcaliphilum reaction of serine-pyruvate aminotransferase (SPAT), EC 2.6.1.51 3-hydroxypyruvate + L-alanine
-
 ?
L-serine + pyruvate Methylococcus capsulatus reaction of serine-pyruvate aminotransferase (SPAT), EC 2.6.1.51 3-hydroxypyruvate + L-alanine
-
 ?
L-serine + pyruvate Methylococcus capsulatus Bath reaction of serine-pyruvate aminotransferase (SPAT), EC 2.6.1.51 3-hydroxypyruvate + L-alanine
-
 ?
L-serine + pyruvate Methylotuvimicrobium alcaliphilum VKM B-2133 reaction of serine-pyruvate aminotransferase (SPAT), EC 2.6.1.51 3-hydroxypyruvate + L-alanine
-
 ?
L-serine + pyruvate Methylococcus capsulatus ATCC 33009 reaction of serine-pyruvate aminotransferase (SPAT), EC 2.6.1.51 3-hydroxypyruvate + L-alanine
-
 ?
L-serine + pyruvate Methylotuvimicrobium alcaliphilum 20Z reaction of serine-pyruvate aminotransferase (SPAT), EC 2.6.1.51 3-hydroxypyruvate + L-alanine
-
 ?
L-serine + pyruvate Methylococcus capsulatus NCIMB 11132 reaction of serine-pyruvate aminotransferase (SPAT), EC 2.6.1.51 3-hydroxypyruvate + L-alanine
-
 ?
L-serine + pyruvate Methylotuvimicrobium alcaliphilum DSM 19304 reaction of serine-pyruvate aminotransferase (SPAT), EC 2.6.1.51 3-hydroxypyruvate + L-alanine
-
 ?
L-serine + pyruvate Methylotuvimicrobium alcaliphilum NCIMB 14124 reaction of serine-pyruvate aminotransferase (SPAT), EC 2.6.1.51 3-hydroxypyruvate + L-alanine
-
 ?

Organism

Organism UniProt Comment Textmining
Methylococcus capsulatus Q608T3
-
-
Methylococcus capsulatus ATCC 33009 Q608T3
-
-
Methylococcus capsulatus Bath Q608T3
-
-
Methylococcus capsulatus NCIMB 11132 Q608T3
-
-
Methylosinus trichosporium
-
-
-
Methylotuvimicrobium alcaliphilum G4T3S7
-
-
Methylotuvimicrobium alcaliphilum 20Z G4T3S7
-
-
Methylotuvimicrobium alcaliphilum DSM 19304 G4T3S7
-
-
Methylotuvimicrobium alcaliphilum NCIMB 14124 G4T3S7
-
-
Methylotuvimicrobium alcaliphilum VKM B-2133 G4T3S7
-
-

Purification (Commentary)

Purification (Comment) Organism
recombinant His-tagged enzyme from Escherichia coli strain Rosetta (DE3) by nickel affinity chromatography Methylosinus trichosporium
recombinant His-tagged enzyme from Escherichia coli strain Rosetta (DE3) by nickel affinity chromatography Methylotuvimicrobium alcaliphilum
recombinant His-tagged enzyme from Escherichia coli strain Rosetta (DE3) by nickel affinity chromatography Methylococcus capsulatus

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
L-alanine + glyoxylate reaction of alanine-glyoxylate aminotransferase (AGAT), EC 2.6.1.44 Methylotuvimicrobium alcaliphilum pyruvate + glycine
-
 ?
L-alanine + glyoxylate reaction of alanine-glyoxylate aminotransferase (AGAT), EC 2.6.1.44 Methylococcus capsulatus pyruvate + glycine
-
 ?
L-alanine + glyoxylate reaction of alanine-glyoxylate aminotransferase (AGAT), EC 2.6.1.44 Methylococcus capsulatus Bath pyruvate + glycine
-
 ?
L-alanine + glyoxylate reaction of alanine-glyoxylate aminotransferase (AGAT), EC 2.6.1.44 Methylotuvimicrobium alcaliphilum VKM B-2133 pyruvate + glycine
-
 ?
L-alanine + glyoxylate reaction of alanine-glyoxylate aminotransferase (AGAT), EC 2.6.1.44 Methylococcus capsulatus ATCC 33009 pyruvate + glycine
-
 ?
L-alanine + glyoxylate reaction of alanine-glyoxylate aminotransferase (AGAT), EC 2.6.1.44 Methylotuvimicrobium alcaliphilum 20Z pyruvate + glycine
-
 ?
L-alanine + glyoxylate reaction of alanine-glyoxylate aminotransferase (AGAT), EC 2.6.1.44 Methylococcus capsulatus NCIMB 11132 pyruvate + glycine
-
 ?
L-alanine + glyoxylate reaction of alanine-glyoxylate aminotransferase (AGAT), EC 2.6.1.44 Methylotuvimicrobium alcaliphilum DSM 19304 pyruvate + glycine
-
 ?
L-alanine + glyoxylate reaction of alanine-glyoxylate aminotransferase (AGAT), EC 2.6.1.44 Methylotuvimicrobium alcaliphilum NCIMB 14124 pyruvate + glycine
-
 ?
L-serine + 2-oxoglutarate
-
 Methylotuvimicrobium alcaliphilum 3-hydroxypyruvate + L-glutamate
-
 ?
L-serine + 2-oxoglutarate
-
 Methylococcus capsulatus 3-hydroxypyruvate + L-glutamate
-
 ?
L-serine + 2-oxoglutarate
-
 Methylococcus capsulatus Bath 3-hydroxypyruvate + L-glutamate
-
 ?
L-serine + 2-oxoglutarate
-
 Methylotuvimicrobium alcaliphilum VKM B-2133 3-hydroxypyruvate + L-glutamate
-
 ?
L-serine + 2-oxoglutarate
-
 Methylococcus capsulatus ATCC 33009 3-hydroxypyruvate + L-glutamate
-
 ?
L-serine + 2-oxoglutarate
-
 Methylotuvimicrobium alcaliphilum 20Z 3-hydroxypyruvate + L-glutamate
-
 ?
L-serine + 2-oxoglutarate
-
 Methylococcus capsulatus NCIMB 11132 3-hydroxypyruvate + L-glutamate
-
 ?
L-serine + 2-oxoglutarate
-
 Methylotuvimicrobium alcaliphilum DSM 19304 3-hydroxypyruvate + L-glutamate
-
 ?
L-serine + 2-oxoglutarate
-
 Methylotuvimicrobium alcaliphilum NCIMB 14124 3-hydroxypyruvate + L-glutamate
-
 ?
L-serine + glyoxylate preferred substrates Methylosinus trichosporium 3-hydroxypyruvate + glycine
-
 ?
L-serine + glyoxylate preferred substrates Methylotuvimicrobium alcaliphilum 3-hydroxypyruvate + glycine
-
 ?
L-serine + glyoxylate preferred substrates Methylococcus capsulatus 3-hydroxypyruvate + glycine
-
 ?
L-serine + glyoxylate preferred substrates Methylococcus capsulatus Bath 3-hydroxypyruvate + glycine
-
 ?
L-serine + glyoxylate preferred substrates Methylotuvimicrobium alcaliphilum VKM B-2133 3-hydroxypyruvate + glycine
-
 ?
L-serine + glyoxylate preferred substrates Methylococcus capsulatus ATCC 33009 3-hydroxypyruvate + glycine
-
 ?
L-serine + glyoxylate preferred substrates Methylotuvimicrobium alcaliphilum 20Z 3-hydroxypyruvate + glycine
-
 ?
L-serine + glyoxylate preferred substrates Methylococcus capsulatus NCIMB 11132 3-hydroxypyruvate + glycine
-
 ?
L-serine + glyoxylate preferred substrates Methylotuvimicrobium alcaliphilum DSM 19304 3-hydroxypyruvate + glycine
-
 ?
L-serine + glyoxylate preferred substrates Methylotuvimicrobium alcaliphilum NCIMB 14124 3-hydroxypyruvate + glycine
-
 ?
L-serine + pyruvate reaction of serine-pyruvate aminotransferase (SPAT), EC 2.6.1.51 Methylosinus trichosporium 3-hydroxypyruvate + L-alanine
-
 ?
L-serine + pyruvate reaction of serine-pyruvate aminotransferase (SPAT), EC 2.6.1.51 Methylotuvimicrobium alcaliphilum 3-hydroxypyruvate + L-alanine
-
 ?
L-serine + pyruvate reaction of serine-pyruvate aminotransferase (SPAT), EC 2.6.1.51 Methylococcus capsulatus 3-hydroxypyruvate + L-alanine
-
 ?
L-serine + pyruvate reaction of serine-pyruvate aminotransferase (SPAT), EC 2.6.1.51 Methylococcus capsulatus Bath 3-hydroxypyruvate + L-alanine
-
 ?
L-serine + pyruvate reaction of serine-pyruvate aminotransferase (SPAT), EC 2.6.1.51 Methylotuvimicrobium alcaliphilum VKM B-2133 3-hydroxypyruvate + L-alanine
-
 ?
L-serine + pyruvate reaction of serine-pyruvate aminotransferase (SPAT), EC 2.6.1.51 Methylococcus capsulatus ATCC 33009 3-hydroxypyruvate + L-alanine
-
 ?
L-serine + pyruvate reaction of serine-pyruvate aminotransferase (SPAT), EC 2.6.1.51 Methylotuvimicrobium alcaliphilum 20Z 3-hydroxypyruvate + L-alanine
-
 ?
L-serine + pyruvate reaction of serine-pyruvate aminotransferase (SPAT), EC 2.6.1.51 Methylococcus capsulatus NCIMB 11132 3-hydroxypyruvate + L-alanine
-
 ?
L-serine + pyruvate reaction of serine-pyruvate aminotransferase (SPAT), EC 2.6.1.51 Methylotuvimicrobium alcaliphilum DSM 19304 3-hydroxypyruvate + L-alanine
-
 ?
L-serine + pyruvate reaction of serine-pyruvate aminotransferase (SPAT), EC 2.6.1.51 Methylotuvimicrobium alcaliphilum NCIMB 14124 3-hydroxypyruvate + L-alanine
-
 ?

Subunits

Subunits Comment Organism
homodimer 4 * 45000, SDS-PAGE Methylosinus trichosporium
homodimer 2 * 40000, SDS-PAGE Methylotuvimicrobium alcaliphilum
homotrimer 3 * 40000, SDS-PAGE Methylococcus capsulatus

Synonyms

Synonyms Comment Organism
More see also EC 2.6.1.44 and EC 2.6.1.51 Methylotuvimicrobium alcaliphilum
More see also EC 2.6.1.51 Methylosinus trichosporium
More see also EC 2.6.1.51 and 2.6.1.44 Methylococcus capsulatus
serine-alpha-ketoglutarate aminotransferase
-
 Methylotuvimicrobium alcaliphilum
serine-alpha-ketoglutarate aminotransferase
-
 Methylococcus capsulatus
serine-glyoxylate aminotranferase
-
 Methylosinus trichosporium
serine-glyoxylate aminotranferase
-
 Methylococcus capsulatus
serine-glyoxylate aminotransferase
-
 Methylotuvimicrobium alcaliphilum
Sga
-
 Methylosinus trichosporium
Sga
-
 Methylotuvimicrobium alcaliphilum
Sga
-
 Methylococcus capsulatus
Sga20Z
-
 Methylotuvimicrobium alcaliphilum
SgaBath
-
 Methylococcus capsulatus
SGAT
-
 Methylotuvimicrobium alcaliphilum
SGAT
-
 Methylococcus capsulatus
SKAT
-
 Methylotuvimicrobium alcaliphilum
SKAT
-
 Methylococcus capsulatus

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7
-
-
 Methylosinus trichosporium
7
-
-
 Methylococcus capsulatus
7.5
-
-
 Methylotuvimicrobium alcaliphilum

Cofactor

Cofactor Comment Organism Structure
pyridoxal 5'-phosphate PLP Methylosinus trichosporium
pyridoxal 5'-phosphate PLP Methylotuvimicrobium alcaliphilum
pyridoxal 5'-phosphate PLP Methylococcus capsulatus

General Information

General Information Comment Organism
evolution phylogenetic analysis and tree Methylosinus trichosporium
evolution phylogenetic analysis and tree Methylotuvimicrobium alcaliphilum
evolution phylogenetic analysis and tree Methylococcus capsulatus
malfunction the disruption of the sga gene in Methylomicrobium alcaliphilum results in retardation of growth rate of the mutant cells and in a prolonged lag-phase after passaging from methane to methanol. In addition, the growth of the mutant strain is accompanied by formaldehyde accumulation in the culture liquid Methylotuvimicrobium alcaliphilum
metabolism serine-glyoxylate aminotransferase (Sga) is the indicator enzyme of the serine pathway of assimilation of reduced C1 compounds Methylosinus trichosporium
metabolism serine-glyoxylate aminotransferase (Sga) is the indicator enzyme of the serine pathway of assimilation of reduced C1 compounds Methylotuvimicrobium alcaliphilum
metabolism serine-glyoxylate aminotransferase (Sga) is the indicator enzyme of the serine pathway of assimilation of reduced C1 compounds Methylococcus capsulatus
additional information influence of metabolites on the activity of recombinant serineglyoxylate aminotransferase, overview Methylosinus trichosporium
additional information influence of metabolites on the activity of recombinant serineglyoxylate aminotransferase, overview Methylotuvimicrobium alcaliphilum
additional information influence of metabolites on the activity of recombinant serineglyoxylate aminotransferase, overview Methylococcus capsulatus
physiological function serine-glyoxylate aminotransferase (Sga) is the indicator enzyme of the serine pathway of assimilation of reduced C1 compounds. The Sga enzyme from the methanotroph catalyses the pyridoxal phosphate-dependent transfer of an amino group from serine to glyoxylate and pyruvate. Enzyme Sga is important in the serine cycle of type I methanotrophs and this pathway might be related to the removal of excess formaldehyde and/or energy regulation Methylosinus trichosporium
physiological function serine-glyoxylate aminotransferase (Sga) is the indicator enzyme of the serine pathway of assimilation of reduced C1 compounds. The Sga enzyme from the methanotroph catalyses the pyridoxal phosphate-dependent transfer of an amino group from serine to glyoxylate and pyruvate. The enzyme also transfers an amino group from serine to 2-oxoglutarate and from alanine to glyoxylate. Enzyme Sga is important in the serine cycle of type I methanotrophs and this pathway might be related to the removal of excess formaldehyde and/or energy regulation Methylotuvimicrobium alcaliphilum
physiological function serine-glyoxylate aminotransferase (Sga) is the indicator enzyme of the serine pathway of assimilation of reduced C1 compounds. The Sga enzyme from the methanotroph catalyses the pyridoxal phosphate-dependent transfer of an amino group from serine to glyoxylate and pyruvate. The enzyme also transfers an amino group from serine to 2-oxoglutarate and from alanine to glyoxylate. Enzyme Sga is important in the serine cycle of type I methanotrophs and this pathway might be related to the removal of excess formaldehyde and/or energy regulation Methylococcus capsulatus