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"cysteine peptidase"¿¡ ´ëÇÑ °Ë»ö °á°úÀÔ´Ï´Ù. °Ë»ö °á°ú º¸´Â µµÁß¿¡ Tab ۸¦ ´©¸£½Ã¸é °Ë»ö âÀÌ ¼±Åõ˴ϴÙ.
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Cys cyclosporine; cysteine
GGCS gamma-glutamyl cysteine synthetase
MCDU mercaptolactate-cysteine disulfiduria
SPARC cysteine-rich acidic secreted protein
LAP   1) Leukocyte Alkaline Phosphatase
  2) Leucine Amino-Peptidase
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MIP Mitochondrial intermediate peptidase
MPP Mitochondrial processing peptidase
SPase Signal peptidase
TPP I Tripeptidyl peptidase I
TFEC 1,1,2,2-tetrafluoroethyl-L-cysteine
CancerWEB ¿µ¿µ ÀÇÇлçÀü À¯»ç °Ë»ö °á°ú : 15 ÆäÀÌÁö: 2
cysteine carboxypeptidase <enzyme> An enzyme which removes the last peptide bond on a protein (the one at the carboxyl end). Its active site contains the sulphur part of the amino acid cysteine.
(09 Oct 1997)
cysteine conjugate S-oxidase <enzyme> Converts s-benzyl-l-cysteine to s-benzyl-l-cysteine sulfoxide; uses o2 and NADPH; may be a flavin-containing monooxygenase
Registry number: EC 1.13.12-
(26 Jun 1999)
cysteine conjugate transaminase <enzyme> Generates thiopyruvates by deamination of cysteine conjugates leaving the r-s-c bond intact
Registry number: EC 2.6.1.-
Synonym: cysteine-conjugate alpha-ketoglutarate transaminase
(26 Jun 1999)
cysteine desulfhydrase <enzyme> A multifunctional pyridoxal phosphate enzyme. In the final step in the biosynthesis of cysteine it catalyses the cleavage of cystathionine to yield cysteine, ammonia, and 2-ketobutyrate.
Chemical name: L-Cystathionine cysteine-lyase (deaminating)
Registry number: EC 4.4.1.1
(12 Dec 1998)
cysteine desulfurase <enzyme> Pyridoxal phosphate enzyme which catalyses the formation of l-alanine and elemental sulfur from cysteine; required for full activation of the metalloproteins of azotobacter vinelandii nitrogenase
Registry number: EC 4.4.1.-
Synonym: nifs gene product, azotobacter, nifs protein, azotobacter
(26 Jun 1999)
cysteine proteinase <enzyme> An enzyme that destroys proteins by hydrolysis, turning them back into individual amino acids.
(09 Oct 1997)
cysteine proteinase inhibitors Exogenous and endogenous compounds which inhibit cysteine proteinases.
(12 Dec 1998)
cysteine proteinases <enzyme> Peptide hydrolases which have a cysteine involved in the catalytic process. This group of enzymes is inactivated by sulfhydryl reagents.
Registry number: EC 3.4.22
(12 Dec 1998)
cysteine S-conjugate N-acetyltransferase <enzyme> Catalyses n-acetylation of l-cysteine thioesters to form mercapturic acids; important in drug detoxication
Registry number: EC 2.3.1.80
Synonym: cscn acetyltransferase
(26 Jun 1999)
cysteine string protein <protein> (CSPs) Peripheral membrane proteins that contain more than 10 palmitoylated cysteines and a DNA J homology domain. Nature 375:647
(18 Nov 1997)
cysteine sulfinate desulfinase <enzyme> Catalyses removal of elemental sulfur and selenium atoms from cysteine, cystine, selenocysteine and selenocystine to produce l-alanine.
Registry number: EC 4.4.1.-
(26 Jun 1999)
cysteine sulfinic acid -O2S-CH2CH (NH3)+COO-;a natural oxidation product of cysteine; an intermediate in the formation of taurine (via cysteic acid).
(05 Mar 2000)
cysteine synthase <enzyme> An enzyme that catalyses the biosynthesis of cysteine in microorganisms and plants from o-acetyl-l-serine and hydrogen sulfide.
Chemical name: O(3)-Acetyl-L-serine acetate-lyase (adding hydrogen sulfide)
Registry number: EC 4.2.99.8
(12 Dec 1998)
procollagen peptidase <enzyme> The proteases that remove the terminal extension peptides of procollagen, deficiency of these enzymes leads to dermatosparaxis or Ehlers Danlos syndrome.
(18 Nov 1997)
pyroglutamyl-peptidase I <enzyme> An enzyme that catalyses the release of a n-terminal pyroglutamyl group from a polypeptide provided the next residue is not proline. It is inhibited by thiol-blocking reagents and occurs in mammalian tissues, microorganisms, and plants.
Registry number: EC 3.4.19.3
(12 Dec 1998)
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