Page last updated: 2024-10-06

folate transformations I

Proteins (22)

ProteinSynonymsTaxonomy
Glycine dehydrogenase (decarboxylating)EC 1.4.4.2; Glycine cleavage system P-protein; Glycine decarboxylase; Glycine dehydrogenase (aminomethyl-transferring)Escherichia coli K-12
Formyltetrahydrofolate deformylaseEC 3.5.1.10; Formyl-FH(4) hydrolaseEscherichia coli K-12
Methenyltetrahydrofolate cyclohydrolaseEC 3.5.4.9Methylorubrum extorquens AM1
Serine hydroxymethyltransferaseSHMT; Serine methylase; EC 2.1.2.1Escherichia coli K-12
Dihydrolipoyl dehydrogenaseEC 1.8.1.4; Dihydrolipoamide dehydrogenase; E3 component of pyruvate and 2-oxoglutarate dehydrogenases complexes; Glycine cleavage system L proteinEscherichia coli K-12
Serine hydroxymethyltransferaseSHMT; Serine methylase; EC 2.1.2.1Hyphomicrobium methylovorum
5-formyltetrahydrofolate cyclo-ligase5-FCL; EC 6.3.3.2; 5,10-methenyltetrahydrofolate synthetase; MTHFSEscherichia coli K-12
AminomethyltransferaseEC 2.1.2.10; Glycine cleavage system T proteinEscherichia coli K-12
Methionine synthaseEC 2.1.1.13; 5-methyltetrahydrofolate--homocysteine methyltransferase; Methionine synthase, vitamin-B12-dependent; MSEscherichia coli K-12
Formate--tetrahydrofolate ligaseEC 6.3.4.3; Formyltetrahydrofolate synthetase; FHS; FTHFSMoorella thermoacetica
Formate--tetrahydrofolate ligaseEC 6.3.4.3; Formyltetrahydrofolate synthetase; FHS; FTHFSMethylorubrum extorquens AM1
5,10-methylenetetrahydrofolate reductaseEC 1.5.1.20Escherichia coli K-12
Glycine cleavage system H proteinEscherichia coli K-12
Bifunctional protein FolDEscherichia coli K-12
Bifunctional protein FolDMoorella thermoacetica ATCC 39073
Methylenetetrahydrofolate reductase Moorella thermoacetica ATCC 39073
Uncharacterized proteinMoorella thermoacetica ATCC 39073
F420-non-reducing hydrogenase subunit DMoorella thermoacetica ATCC 39073
Zinc-finger proteinMoorella thermoacetica ATCC 39073
Heterodisulfide reductase, C subunitMoorella thermoacetica ATCC 39073
Bifunctional protein MdtAMethylorubrum extorquens AM1
4Fe-4S ferredoxin, iron-sulfur binding proteinMoorella thermoacetica ATCC 39073

Compounds (25)

CompoundDescription
hydronium ion
dimethyl sulfidestructure
NADH
Ammonium
CalciumA basic element found in nearly all tissues. It is a member of the alkaline earth family of metals with the atomic symbol Ca, atomic number 20, and atomic weight 40. Calcium is the most abundant mineral in the body and combines with phosphorus to form calcium phosphate in the bones and teeth. It is essential for the normal functioning of nerves and muscles and plays a role in blood coagulation (as factor IV) and in many enzymatic processes.
Carbon DioxideA colorless, odorless gas that can be formed by the body and is necessary for the respiration cycle of plants and animals.
chlorineAn element with atomic symbol Cl, atomic number 17, and atomic weight 35, and member of the halogen family.
ZincA metallic element of atomic number 30 and atomic weight 65.38. It is a necessary trace element in the diet, forming an essential part of many enzymes, and playing an important role in protein synthesis and in cell division. Zinc deficiency is associated with ANEMIA, short stature, HYPOGONADISM, impaired WOUND HEALING, and geophagia. It is known by the symbol Zn.
Orthophosphate
Flavin MononucleotideA coenzyme for a number of oxidative enzymes including NADH DEHYDROGENASE. It is the principal form in which RIBOFLAVIN is found in cells and tissues.
adenosine diphosphateAdenosine 5'-(trihydrogen diphosphate). An adenine nucleotide containing two phosphate groups esterified to the sugar moiety at the 5'-position.
potassiumAn element in the alkali group of metals with an atomic symbol K, atomic number 19, and atomic weight 39.10. It is the chief cation in the intracellular fluid of muscle and other cells. Potassium ion is a strong electrolyte that plays a significant role in the regulation of fluid volume and maintenance of the WATER-ELECTROLYTE BALANCE.
SodiumA member of the alkali group of metals. It has the atomic symbol Na, atomic number 11, and atomic weight 23.
WaterA clear, odorless, tasteless liquid that is essential for most animal and plant life and is an excellent solvent for many substances. The chemical formula is hydrogen oxide (H2O). (McGraw-Hill Dictionary of Scientific and Technical Terms, 4th ed)
adenosine 5'-O-(3-thiotriphosphate)RN given refers to cpd with unspecified locant for thio group; see also records for 1-thio & 2-thio-isomers
trimethylsulfoniuminhibitor of a trimethylamine mono-oxygenase; RN given refers to parent cpd
mercaptoethanolA water-soluble thiol derived from hydrogen sulfide and ethanol. It is used as a reducing agent for disulfide bonds and to protect sulfhydryl groups from oxidation.
nadA coenzyme composed of ribosylnicotinamide 5'-diphosphate coupled to adenosine 5'-phosphate by pyrophosphate linkage. It is found widely in nature and is involved in numerous enzymatic reactions in which it serves as an electron carrier by being alternately oxidized (NAD+) and reduced (NADH). (Dorland, 27th ed)
NADPNicotinamide adenine dinucleotide phosphate. A coenzyme composed of ribosylnicotinamide 5'-phosphate (NMN) coupled by pyrophosphate linkage to the 5'-phosphate adenosine 2',5'-bisphosphate. It serves as an electron carrier in a number of reactions, being alternately oxidized (NADP+) and reduced (NADPH). (Dorland, 27th ed)
NADPNicotinamide adenine dinucleotide phosphate. A coenzyme composed of ribosylnicotinamide 5'-phosphate (NMN) coupled by pyrophosphate linkage to the 5'-phosphate adenosine 2',5'-bisphosphate. It serves as an electron carrier in a number of reactions, being alternately oxidized (NADP+) and reduced (NADPH). (Dorland, 27th ed)
formate
glyoxylate
adenosine triphosphateAn adenine nucleotide containing three phosphate groups esterified to the sugar moiety. In addition to its crucial roles in metabolism adenosine triphosphate is a neurotransmitter.
methyl methanethiosulfonate
Flavin-Adenine DinucleotideA condensation product of riboflavin and adenosine diphosphate. The coenzyme of various aerobic dehydrogenases, e.g., D-amino acid oxidase and L-amino acid oxidase. (Lehninger, Principles of Biochemistry, 1982, p972)