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 ?
Prolonged treatment with N-acetyl cysteine and L-arginine restores gonadal function in patients with PCO syndrome.
The analysis of 531 bp of the cysteine protease genes, when compared with the reported sequence of the Nigerian I/CDC, showed that variant isolates differed at 19 bp (3.
Relationships among plasma homocysteine, cysteine, and albumin concentrations: potential utility of assessing the cysteine/homocysteine ratio.
Chapter Four Cysteine Methyl Ester Development Policy and Plan
METHODS: Rats were allocated to four groups: control (normal drinking water), 1% methylglyoxal in drinking water, 1% methylglyoxal plus N-acetyl cysteine (NAC) (800 mg/kg per day), a methylglyoxal scavenger, or TM2002 (100 mg/kg per day), an advanced glycation endproducts (AGEs) inhibitor.
Plasma concentrations of total cysteine (tCys), total homocysteine (tHcy), and total cysteinylglycine (tCysGly) in 195 umbilical cord (102 males and 92 females; no gender was recorded for 1 neonate) and 35 maternal samples were determined by HPLC as described previously (2).
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Cysteine, which is mainly acquired through diet, can be toxic at high levels, so the production of pheomelanin may help to sequester excess quantities of this amino acid.
These results confirm that GSH deficiency is characteristic of edematous PEM [protein-energy malnutrition] and suggest that this is due to a reduced rate of synthesis secondary to a shortage in cysteine.
A: Cysteine is a sulfur-based amino acid (part of protein) that helps protect your brain and liver from heavy metals and damage from pharmaceutical drugs, chemotherapy, radiation treatment, smoking, and alcohol.
The researchers caution that simply eating cheese will not ensure an increase in glutathione levels, because cysteine is contained in the whey that is separated from cheese early in the cheese-making process.
In this conformation, the enzyme must be inactive since the catalytic cysteine is no longer positioned in the ligand-binding pocket.