Alanine metabolism (Homo sapiens)

Quality Tags

Ontology Terms

Saving...

Bibliography

1. Ishiguro M, Takio K, Suzuki M, Oyama R, Matsuzawa T, Titani K.; ''Complete amino acid sequence of human liver cytosolic alanine aminotransferase (GPT) determined by a combination of conventional and mass spectral methods.''; PubMed Europe PMC Scholia
2. Owen OE, Reichard GA, Patel MS, Boden G.; ''Energy metabolism in feasting and fasting.''; PubMed Europe PMC Scholia
3. Felig P.; ''Amino acid metabolism in man.''; PubMed Europe PMC Scholia
4. Yang RZ, Blaileanu G, Hansen BC, Shuldiner AR, Gong DW.; ''cDNA cloning, genomic structure, chromosomal mapping, and functional expression of a novel human alanine aminotransferase.''; PubMed Europe PMC Scholia
5. Glinghammar B, Rafter I, Lindström AK, Hedberg JJ, Andersson HB, Lindblom P, Berg AL, Cotgreave I.; ''Detection of the mitochondrial and catalytically active alanine aminotransferase in human tissues and plasma.''; PubMed Europe PMC Scholia
6. Sohocki MM, Sullivan LS, Harrison WR, Sodergren EJ, Elder FF, Weinstock G, Tanase S, Daiger SP.; ''Human glutamate pyruvate transaminase (GPT): localization to 8q24.3, cDNA and genomic sequences, and polymorphic sites.''; PubMed Europe PMC Scholia

History

External references

DataNodes

Name	Type	Database reference	Comment
2OG	Metabolite	CHEBI:16810 (ChEBI)
L-Ala	Metabolite	CHEBI:57972 (ChEBI)
L-Glu	Metabolite	CHEBI:29985 (ChEBI)
PXLP-K314-GPT	Protein	P24298 (Uniprot-TrEMBL)
PXLP-K314-GPT dimer	Complex	R-HSA-70521 (Reactome)
PXLP-K341-GPT2 dimer	Complex	R-HSA-507753 (Reactome)
PXLP-K341-GPT2-1	Protein	Q8TD30-1 (Uniprot-TrEMBL)
PYR	Metabolite	CHEBI:15361 (ChEBI)

Annotated Interactions

Source	Target	Type	Database reference	Comment
	2OG	Arrow	R-HSA-507749 (Reactome)
	2OG	Arrow	R-HSA-70524 (Reactome)
2OG			R-HSA-507775 (Reactome)
2OG			R-HSA-70523 (Reactome)
	L-Ala	Arrow	R-HSA-507749 (Reactome)
	L-Ala	Arrow	R-HSA-70524 (Reactome)
L-Ala			R-HSA-507775 (Reactome)
L-Ala			R-HSA-70523 (Reactome)
	L-Glu	Arrow	R-HSA-507775 (Reactome)
	L-Glu	Arrow	R-HSA-70523 (Reactome)
L-Glu			R-HSA-507749 (Reactome)
L-Glu			R-HSA-70524 (Reactome)
PXLP-K314-GPT dimer		mim-catalysis	R-HSA-70523 (Reactome)
PXLP-K314-GPT dimer		mim-catalysis	R-HSA-70524 (Reactome)
PXLP-K341-GPT2 dimer		mim-catalysis	R-HSA-507749 (Reactome)
PXLP-K341-GPT2 dimer		mim-catalysis	R-HSA-507775 (Reactome)
	PYR	Arrow	R-HSA-507775 (Reactome)
	PYR	Arrow	R-HSA-70523 (Reactome)
PYR			R-HSA-507749 (Reactome)
PYR			R-HSA-70524 (Reactome)
			R-HSA-507749 (Reactome)	Glutamic-pyruvate transaminase 2 (alanine aminotransferase 2) (GPT2) catalyzes the reversible reaction of pyruvate and glutamate to form alanine and 2-oxoglutarate (alpha-ketoglutarate) (Yang et al. 2002). Unpublished crystallographic data are consistent with a homodimeric structure for the enzyme with one molecule of pyridoxal phosphate associated with each monomer (PDB 3IHJ). Recent studies of organelles purified from cultured human muscle cells suggest that GPT2 is localized to mitochondria (Glinghammar et al. 2009).
			R-HSA-507775 (Reactome)	Glutamic-pyruvate transaminase 2 (alanine aminotransferase 2) (GPT2) catalyzes the reversible reaction of alanine and 2-oxoglutarate (alpha-ketoglutarate) to form pyruvate and glutamate (Yang et al. 2002). Unpublished crystallographic data are consistent with a homodimeric structure for the enzyme with one molecule of pyridoxal phosphate associated with each monomer (PDB 3IHJ). Recent studies of organelles purified from cultured human muscle cells suggest that GPT2 is localized to mitochondria (Glinghammar et al. 2009).
			R-HSA-70523 (Reactome)	Cytosolic glutamic-pyruvate transaminase (alanine aminotransferase) (GPT) catalyzes the reversible reaction of alanine and 2-oxoglutarate (alpha-ketoglutarate) to form pyruvate and glutamate (Sohocki et al. 1997; Yang et al. 2002). The active form of the enzyme is a dimer (Ishiguro et al. 1991) and is inferred to have a molecule of pyridoxal phosphate associated with each monomer. This reaction allows the synthesis of alanine from intermediates of glucose metabolism in a well-fed person. Under fasting conditions, alanine, derived from protein breakdown, can be converted to pyruvate and used to synthesize glucose via the gluconeogenic pathway in liver, or fully oxidized via the TCA cycle in other tissues.
			R-HSA-70524 (Reactome)	Cytosolic glutamic-pyruvate transaminase (alanine aminotransferase) (GPT) catalyzes the reversible reaction of pyruvate and glutamate to form alanine and 2-oxoglutarate (alpha-ketoglutarate) (Sohocki et al. 1997; Yang et al. 2002). The active form of the enzyme is a dimer (Ishiguro et al. 1991) and is inferred to have a molecule of pyridoxal phosphate associated with each monomer. This reaction allows the synthesis of alanine from intermediates of glucose metabolism in a well-fed person. Under fasting conditions, alanine, derived from protein breakdown, can be converted to pyruvate and used to synthesize glucose via the gluconeogenic pathway in liver, or fully oxidized via the TCA cycle in other tissues.