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HEMITHIOACETAL

Hemithioacetal

Organosulfur compound of the form –CH(–OH)S–

In organic chemistry, hemithioacetals (or thiohemiacetals) are organosulfur compounds with the general formula R−CH(−OH)−SR’. They are the sulfur analogues

Hemithioacetal

Thioacetal

Organosulfur compounds of the form –CH(O–)S– or –CH(S–)2

reactions proceed via the intermediacy of hemithioacetals (R−CH(−OH)−SR'): Thiol addition to give hemithioacetal: RSH + R'CH(O) → R'CH(SR)OH Thiol addition

Thioacetal

Lactoylglutathione lyase

Protein-coding gene in the species Homo sapiens

4.4.1.5, also known as glyoxalase I) catalyzes the isomerization of hemithioacetal adducts, which are formed in a spontaneous reaction between a glutathionyl

Lactoylglutathione lyase

Lactoylglutathione_lyase

Glyceraldehyde 3-phosphate dehydrogenase

Enzyme of the glycolysis metabolic pathway

attacks the carbonyl group of G3P, creating a hemithioacetal intermediate (covalent catalysis). The hemithioacetal is deprotonated by a histidine residue in

Glyceraldehyde 3-phosphate dehydrogenase

Glyceraldehyde_3-phosphate_dehydrogenase

Methylglyoxal

Chemical compound

detoxified by glutathione. Glutathione reacts with methylglyoxal to give a hemithioacetal, which converted into S-D-lactoyl-glutathione by glyoxalase I. This

Methylglyoxal

Glyoxalase system

Biochemistry; detoxification enzyme system

glyoxalase І catalyzes the isomerization of the spontaneously formed hemithioacetal adduct between glutathione and 2-oxoaldehydes (such as methylglyoxal)

Glyoxalase system

Glyoxalase_system

Sulfanegen

Chemical compound

clinically effective. Instead, alternative chemicals such as sulfanegen, the hemithioacetal cyclic dimer of 3-MP, are being evaluated that produce 3-MP in vivo

Sulfanegen

DJ-1

Protein-coding gene found in humans

However, since the steady-state kinetics of DJ-1 acting on reversible hemithioacetal substrates are fitted adequately with a computational kinetic model

DJ-1

MROH9

Mammalian gene

lactoylglutathione ligase, is an enzyme catalyzing isomerization of hemithioacetal adducts. These results explain that MROH9 function may depend on the

MROH9

Dynamic combinatorial chemistry

identification of β-galactosidase inhibitors from a virtual dynamic hemithioacetal system". Angew. Chem. Int. Ed. 49 (3): 589–593. Bibcode:2010ACIE...49

Dynamic combinatorial chemistry

Dynamic_combinatorial_chemistry

Prenylcysteine oxidase

lyase. Prenylcysteine oxidase 1, symbol PCYOX1, gene on chromosome 2 Hemithioacetals in nature, for mechanism of action Flavin adenine dinucleotide, cofactor

Prenylcysteine oxidase

Prenylcysteine_oxidase