cysteine


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Related to cysteine: methionine, cytosine

cysteine

 [sis-te´ēn]
a sulfur-containing amino acid, one of the nonessential amino acids, produced by enzymatic or acid hydrolysis of proteins; it is readily oxidized to cystine and is sometimes found in urine.

cys·te·ine (C, Cys),

(sis-tē'in), Do not confuse this word with cystine.
l-isomer of this acid is found in most proteins; especially abundant in keratin.

cysteine

/cys·te·ine/ (sis-te´ēn) a sulfur-containing, nonessential amino acid produced by enzymatic or acid hydrolysis of proteins, readily oxidized to cystine; sometimes found in urine. Symbols Cys and C.

cysteine

(sĭs′tə-ēn′, -ĭn, -tē-)
n.
An amino acid, C3H7O2NS, derived from cystine and found in most proteins.

cysteine (Cys)

[sis′tēn]
an amino acid containing a polar side chain found in many proteins in the body, including keratin. It is a metabolic precursor of cystine and an important source of sulfur for various body functions. Compare cystine.
enlarge picture
Chemical structure of cysteine

cys·te·ine

(C, Cys) (sis-tē'in)
An amino acid found in most proteins; especially abundant in keratin.

cysteine

An AMINO ACID present in most body proteins.
Cysteineclick for a larger image
Fig. 125 Cysteine . Molecular structure.

cysteine (C, Cys)

one of 20 AMINO ACIDS common in proteins that has a polar ‘R’ structure and is water-soluble. See Fig. 125 . The R group contains a sulphydryl (SH) group which is vital for the formation of DISULPHIDE BRIDGES in proteins. Disulphide bridges hold polypeptides together and give stability, especially in molecules such as KERATIN and IMMUNOGLOBULINS. The ISOELECTRIC POINT of cysteine is 5.1.

cysteine

amino acid present in most proteins, but especially abundant in keratin

cys·te·ine

(C) (sis-tē'in) Do not confuse this word with cystine.
l-isomer of this acid is found in most proteins; especially abundant in keratin.

cysteine (sis´təēn´),

n a nonessential amino acid found in many proteins in the body.

cysteine

a sulfur-containing amino acid produced by enzymatic or acid hydrolysis of proteins, readily oxidized to cystine; sometimes found in urine.
References in periodicals archive ?
The cholesterol binding sites of PFO lies in its conserved cysteine residue, sandwiched between a b-sheet and Trp 467 [25, 26].
Emerging roles of cysteine cathepsins in disease and their potential as drug targets.
Five microliters of the gastric fluid in reducing conditions were incubated for 1 h in the presence of 5 pi of 1 mM Pefabloc (Fluka 76307), 1 mM E-64 (Sigma-Aldrich E-3132), or 1 mM Pepstatin A (Sigma-Aldrich P-4265) in dimethyl sulfoxide (DMSO, Sigma-Aldrich D-5879), which are specific inhibitors for serine, cysteine, and aspartic peptidases, respectively.
Our current results provide additional mechanistic insights as to how NRG-1 activation of the PI3K/Akt pathway provides neuroprotection against oxidative stress by demonstrating that NRG-1 stimulates cysteine uptake, leading to increased synthesis of GSH, the primary antioxidant in neuronal cells (Figure 3).
Cysteine + homocysteine [right arrow] cystathionine + [H.
Absorbance against reagent blank was measured at 412 nm and cysteine (Sigma Aldrich, Germany) was used as a standard.
1]) on growth, biomass, tissue sulfur, photoassmilatory pigments, cysteine, carbohydrates (sugars and starch), and antioxidative enzymatic and nonenzymatic components were evaluated, and the whole experiment was analysed at two stages 35 and 58 days of after treatment.
This band disappears on encapsulation of Ni NPs with l- cysteine molecules as depicted in (Fig.
While it can protect the tau protein by binding to its vulnerable cysteine residues, it can also come off, Graves added, which can ensure the proper functioning of the protein.
We predicted that if we added isoniazid and cysteine to isoniazid-sensitive M.
In this review, we discuss the chemical nature of ACR (a soft electrophile) and how this determines the corresponding sites of protein adduction (soft nucleophilic sulfhydryl thiolates on cysteine residues).