Literature summary for 2.1.2.1 extracted from

di Salvo, M.L.; Contestabile, R.; Paiardini, A.; Maras, B.
Glycine consumption and mitochondrial serine hydroxymethyltransferase in cancer cells: the heme connection (2013), Med. Hypotheses, 80, 633-636.

Search for more literature for 2.1.2.1

Application

Application	Comment	Organism
drug development	the enzyme might be a a key target for the development of chemotherapic agents	Homo sapiens

Localization

Localization	Comment	Organism	GeneOntology No.	Textmining
mitochondrion	mitochondrial isozyme SHMT2	Homo sapiens	5739	-

Organism

Organism	UniProt	Comment	Textmining
Homo sapiens	P34897	-	-

Synonyms

Synonyms	Comment	Organism
mitochondrial serine hydroxymethyltransferase	-	Homo sapiens
SHMT2	-	Homo sapiens

General Information

General Information	Comment	Organism
malfunction	overexpression of mitochondrial serine hydroxymethyltransferase assures an adequate supply of glycine to rapidly proliferating cancer cells, silencing of mitochondrial serine hydroxymethyltransferase halts cancer cell proliferation and supplementation with sarcosine (a glycine-related metabolite) or formate (a source of one carbon units) fails to rescue cell proliferation	Homo sapiens
physiological function	mitochondrial serine hydroxymethyltransferase seems to be fundamental to sustain cancer metabolism since production of glycine fuels heme biosynthesis and therefore oxidative phosphorylation. Respiration of cancer cells may then ultimately rely on endogenous glycine synthesis by mitochondrial serine hydroxymethyltransferase. The link between mitochondrial serine hydroxymethyltransferase activity and heme biosynthesis represents an important aspect of cancer cell metabolism. Glycine itself, rather than one-carbon units deriving from the SHMT2 reaction, is specifically critical in cancer cells	Homo sapiens

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Release 2023.1 (January 2023)