Search results for MTHFD1

Showing 11 results out of 11

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Protein (2 results from a total of 2)

Identifier: R-HSA-200641
Species: Homo sapiens
Compartment: cytosol
Primary external reference: UniProt: MTHFD1: P11586
Identifier: R-HSA-5696852
Species: Homo sapiens
Compartment: mitochondrial matrix
Primary external reference: UniProt: MTHFD1L: Q6UB35

Complex (2 results from a total of 2)

Identifier: R-HSA-200667
Species: Homo sapiens
Compartment: cytosol
Identifier: R-HSA-5696840
Species: Homo sapiens
Compartment: mitochondrial matrix

Reaction (7 results from a total of 7)

Identifier: R-HSA-200661
Species: Homo sapiens
Compartment: cytosol
The methenyltetrahydrofolate cyclohydrolase activity of the trifunctional MTHFD1 enzyme catalyzes the reversible reaction of 10-formylTHF polyglutamate to form 5,10-methenylTHF polyglutamate and H2O. MTHFD1 is cytosolic and occurs as a dimer. The human enzyme has been identified and partially characterized biochemically (Hum et al. 1988); additional reaction details can be inferred from the properties of the well-studied homologous rabbit enzyme (Villar et al. 1985).
Identifier: R-HSA-200718
Species: Homo sapiens
Compartment: cytosol
The methylenetetrahydrofolate dehydrogenase activity of the trifunctional MTHFD1 enzyme catalyzes the reversible reaction of 5,10-methenylTHF polyglutamate, NADPH, and H+ to form 5,10-methyleneTHF polyglutamate and NADP+. MTHFD1 is cytosolic and occurs as a dimer. The human enzyme has been identified and partially characterized biochemically (Hum et al. 1988); additional reaction details can be inferred from the properties of the well-studied homologous rabbit enzyme (Villar et al. 1985).
Identifier: R-HSA-200711
Species: Homo sapiens
Compartment: cytosol
The formate-tetrahydrofolate ligase activity of the trifunctional MTHFD1 enzyme catalyzes the reaction of THF polyglutamate, formate, and ATP to form 10-formylTHF polyglutamate, ADP, and orthophosphate. MTHFD1 is cytosolic and occurs as a dimer. The human enzyme has been identified and partially characterized biochemically (Hum et al. 1988); additional reaction details can be inferred from the properties of the well-studied homologous rabbit enzyme (Villar et al. 1985).
Identifier: R-HSA-6801456
Species: Homo sapiens
Compartment: mitochondrial matrix
All C1-tetrahydrofolate (C1-THF) synthases characterised to date are trifunctional, containing the activities of 5,10-methylene-THF dehydrogenase, 5,10-methenyl-THF cyclohydrolase, and 10-formyl-THF synthetase. Mitochondrial monofunctional C1-tetrahydrofolate synthase (MTHFD1L) only possesses 10-formyl-THF synthetase activity and it reversibly ligates formate (HCOOH) to tetrahydrofolate (THF), forming 10-formyltetrahydrofolate (10-formyl-THF) (Prasannan et al. 2003, Walkup & Appling 2005). MTHFD1L is functional as a homodimer and could be a missing reaction in one-carbon folate metabolism linking the metabolism of formate from the cytosol to mitochondria (Pike et al. 2010). Under most conditions, the majority of one-carbon units for cytoplasmic processes are derived from mitochondrial formate.
Identifier: R-HSA-5696839
Species: Homo sapiens
Compartment: mitochondrial matrix
All C1-tetrahydrofolate (C1-THF) synthases characterised to date are trifunctional, containing the activities of 5,10-methylene-THF dehydrogenase, 5,10-methenyl-THF cyclohydrolase, and 10-formyl-THF synthetase. Mitochondrial monofunctional C1-tetrahydrofolate synthase (MTHFD1L) only possesses 10-formyl-THF synthetase activity and it reversibly ligates formate (HCOOH) to tetrahydrofolate (THF), forming 10-formyltetrahydrofolate (10-formyl-THF) (Prasannan et al. 2003, Walkup & Appling 2005). MTHFD1L is functional as a homodimer and could be a missing reaction in one-carbon folate metabolism linking the metabolism of formate from the cytosol to mitochondria (Pike et al. 2010).
Identifier: R-HSA-200740
Species: Homo sapiens
Compartment: cytosol
The methenyltetrahydrofolate cyclohydrolase activity of the trifunctional MTHFD1 enzyme catalyzes the reversible reaction of 5,10-methenylTHF polyglutamate and H2O to form 10-formylTHF polyglutamate. MTHFD1 is cytosolic and occurs as a dimer. The human enzyme has been identified and partially characterized biochemically (Hum et al. 1988); additional reaction details can be inferred from the properties of the well-studied homologous rabbit enzyme (Villar et al. 1985).
Identifier: R-HSA-200644
Species: Homo sapiens
Compartment: cytosol
The methylenetetrahydrofolate dehydrogenase activity of the trifunctional MTHFD1 enzyme catalyzes the reversible reaction of 5,10-methyleneTHF polyglutamate and NADP+ to form 5,10-methenylTHF polyglutamate, NADPH, and H+. MTHFD1 is cytosolic and occurs as a dimer. The human enzyme has been identified and partially characterized biochemically (Hum et al. 1988); additional reaction details can be inferred from the properties of the well-studied homologous rabbit enzyme (Villar et al. 1985).
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