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  • carbon disulfide
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  • disulfide
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  • disulfide bond
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  • hydrogen disulfide
    ÀÌȲȭ¼ö¼Ò
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  • disulfide bond
    µð¼³Çǵå°áÇÕ
  • carbon disulfide
    ÀÌȲȭź¼Ò
  • disulfide
    ÀÌȲȭ¹°
  • hydrogen disulfide
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  • carbon disulfide
    ÀÌȲȭ(ì£üÜûù)ź¼Ò.
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    ÀÌȲȭź¼ÒÁßµ¶(¡­ñéÔ¸).
  • disulfide
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  • disulfide bond
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  • disulfide bond
    µð¼³Çǵå<ÀÌȲȭ>°áÇÕ (¡­Ì¿ùê).
  • hydrogen disulfide
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  • nickel disulfide
    ÀÌȲȭ(ì£üÜûù)´ÏÄÌ.
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  • lipoamide
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  • lysyl-lipoamide
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  • disulfide
    ÀÌȲȭ¹°(ì£üÜûùÚª)
  • disulfide bond
    ÀÌȲ°áÇÕ(ì£üÜÌ¿ùê)
  • disulfide bridge
    "ÀÌȲ °¡±³(ì£üÜÊ­Îé), (ÔÒ) disulfide bond"
  • disulfide interchange
    ÀÌȲȭ¹°±³È¯(ì£üÜü§ÚªÎßüµ)
  • disulfide link
    "ÀÌȲ ¿¬°á(ì£üÜÖ§Ì¿), (ÔÒ) disulfide bond"
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DDD AV universal [pacemaker]; defined daily dose; degenerative disc disease; dehydroxydinaphthyl disulfi...
LAD lactic acid dehydrogenase; left anterior descending [artery]; left axis deviation; leukocyte adhesio...
BTDS benzoylthiamine disulfide
DSI deep shock insulin; Depression Status Inventory; disulfide isomerase; Down Syndrome International
SS disulfide; sacrosciatic; saline soak; saline solution; saliva sample; saliva substitute; Salmonella-...
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LipDH Lipoamide dehydrogenase
CS2 Carbon Disulfide
DADS Diallyl disulfide
DMDS Dimethyl disulfide
dsFv Disulfide-stabilized Fv
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  • hydrogen disulfide
    ÀÌȲȭ ¼ö¼Ò
CancerWEB ¿µ¿µ ÀÇÇлçÀü ¸ÂÃã °Ë»ö °á°ú : 1 ÆäÀÌÁö: 1
lipoamide disulfide Oxidised lipoic acid in amide combination with the &vepsilon;-amino group of an l-lysyl residue of pyruvic acid dehydrogenase.
(05 Mar 2000)
CancerWEB ¿µ¿µ ÀÇÇлçÀü À¯»ç °Ë»ö °á°ú : 15 ÆäÀÌÁö: 1
pyruvate dehydrogenase (lipoamide) An oxidoreductase catalyzing conversion of pyruvate and (oxidised) lipoamide to CO2 and S6-acetyldihydrolipoamide in two successive reactions: the first between pyruvate and thiamin pyrophosphate to yield CO2 and alpha-hydroxyethylthiamin pyrophosphate (active pyruvate); the second between the last named and lipoamide to regain the thiamin pyrophosphate and yield S6-acetylhydrolipoamide.
Compare: alpha-ketodecarboxylase.
(05 Mar 2000)
pyruvate dehydrogenase (lipoamide)-phosphatase <enzyme> (pyruvate dehydrogenase (lipoamide))-phosphate phosphohydrolase. A mitochondrial enzyme that catalyses the hydrolytic removal of a phosphate on a specific seryl hydroxyl group of pyruvate dehydrogenase, reactivating the enzyme complex.
Registry number: EC 3.1.3.43
(12 Dec 1998)
(pyruvate dehydrogenase (lipoamide))kinase Registry number: EC 2.7.1.99
Synonym: pyruvate dehydrogenase kinase
(26 Jun 1999)
lipoamide <biochemistry> The functional form of lipoic acid in which the carboxyl group is attached to protein by an amide linkage to a lysine amino group.
(18 Nov 1997)
lipoamide dehydrogenase <enzyme> An enzyme that regenerates lipoamide from the reduced form dihydrolipoamide.
(18 Nov 1997)
lipoamide reductase <enzyme> An enzyme oxidizing dihydrolipoamide at the expense of NAD+; completes the oxidative decarboxylation of pyruvate; a part of several enzyme complexes (e.g., alpha-ketoglutarate dehydrogenase complex). Decreased activity leads to neuronal loss in brain resulting in psychomotor retardation.
Synonym: coenzyme factor, lipoamide dehydrogenase, lipoamide reductase (NADH), lipoyl dehydrogenase.
(05 Mar 2000)
asymmetric disulfide <chemistry> Disulfide which is not symmetric on both sides of the -s-s- linkage; e.g., the disulfide formed between coenzyme A and glutathione or between cysteine and coenzyme A or glutathione.
Synonym: asymmetric disulfide.
(05 Mar 2000)
carbon disulfide <chemical> Carbon disulfide (cs2). A colourless, flammable, poisonous liquid, cs2. It is used as a solvent, and is a counterirritant and has local anaesthetic properties but is not used as such. It is highly toxic with pronounced CNS, haematologic, and dermatologic effects.
Chemical name: Carbon disulfide
(12 Dec 1998)
carbon disulfide poisoning Acute or chronic intoxication by CS2, an industrial condition encountered among rubber workers and makers of artificial silk (rayon) by the viscose process; characterised by insomnia, listlessness, and irritability, followed by paralyses, impaired vision, peptic ulcer, and psychoses.
(05 Mar 2000)
carbon monoxide dehydrogenase disulfide reductase <enzyme> Catalyses a reversible exchange of coash with acetyl-CoA in combination with carbon monoxide dehydrogenase (EC 1.2.99.2)
Registry number: EC 1.8.-
Synonym: co dehydrogenase disulfide reductase, co-dd-reductase
(26 Jun 1999)
glutathione disulfide <chemical> A glutathione derivative that forms when the sulfhydryl side chains of the cysteine residues of two glutathione molecules form a disulfide bond during the course of being oxidised with various oxides and peroxides in cells. Glutathione reductase, with the coupled oxidation of NADPH, reduces gssg to two moles of glutathione.
Chemical name: Bis(gamma-Glutamyl-L-cysteinylglycine) Disulfide
(12 Dec 1998)
periplasmic protein disulfide oxidoreductase <enzyme> Isolated from haemophilus influenzae; may be required for assembly or folding of one or more disulfide-containing cell envelope proteins; ccmg isolated from paracoccus denitrificans
Registry number: EC 1.8.4.-
Synonym: por disulfide oxidoreductase, por gene product, periplasmic oxidoreductase, ccmg gene product
(26 Jun 1999)
mixed disulfide <chemistry> Disulfide which is not symmetric on both sides of the -s-s- linkage; e.g., the disulfide formed between coenzyme A and glutathione or between cysteine and coenzyme A or glutathione.
Synonym: asymmetric disulfide.
(05 Mar 2000)
protein disulfide-isomerase <enzyme> An enzyme that catalyses the rearrangement of disulfide bonds within proteins during folding. It is a monomer identical to one of the subunits of procollagen-proline dioxygenase.
Chemical name: Protein disulfide-isomerase
Registry number: EC 5.3.4.1
(12 Dec 1998)
protein disulfide reductase (glutathione) <enzyme> An enzyme that catalyses the reduction of a protein-disulfide in the presence of glutathione, forming a protein-dithiol. Insulin is one of its substrates.
Chemical name: Glutathione:protein-disulfide oxidoreductase
Registry number: EC 1.8.4.2
(12 Dec 1998)
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