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leucin <physiology> A white, crystalline, nitrogenous substance formed in the decomposition of albuminous matter by pancreatic digestion, by the action of boiling dilute sulphuric acid, and by putrefaction. It is also found as a constituent of various tissues and organs, as the spleen, pancreas, etc, and likewise in the vegetable kingdom. Chemically it is to be considered as amido-caproic acid.
Origin: Gr. White.
Source: Websters Dictionary
(01 Mar 1998)
leucine <amino acid> The most abundant amino acid found in proteins. Confers hydrophobicity and has a structural rather than a chemical role.
(18 Nov 1997)
leucine 2,3-aminomutase <enzyme> Leucine is converted to 3-amino-4-methylpentanoate (beta leucine)
Registry number: EC 5.4.3.7
(26 Jun 1999)
leucine acetyltransferase <enzyme> Forms acetyl-l-leucine from acetyl-CoA plus leucine
Registry number: EC 2.3.1.-
Synonym: leucine acyltransferase
(26 Jun 1999)
leucine aminopeptidase <enzyme> An exopeptidase that removes neutral amino acid residues from the N terminus of proteins.
(18 Nov 1997)
leucine dehydrogenase <enzyme> An enzyme that catalyses the reaction of l-leucine, water, and NAD+ to produce NADH, ammonia, and 4-methyl-2-oxopentanoate; used in the treatment of certain tumours.
(05 Mar 2000)
leucine hypoglycaemia Reduction in blood glucose concentration produced by administration of leucine; believed to reflect the ability of this amino acid to stimulate insulin secretion.
(05 Mar 2000)
leucine zipper <molecular biology> Motif found in certain DNA binding proteins. In a region of approximately 35 amino acids, every seventh is a leucine. This facilitates dimerisation of two such proteins to form a functional transcription factor.
Examples of proteins containing leucine zippers are products of the proto-oncogenes myc, fos and jun.
(15 Oct 1997)
leucine zippers Domains in DNA-binding proteins that contain amino acid sequences that show periodic arrays of leucine residues. These residues exist in an alpha-helical conformation, with the leucine side chains extending from one alpha helix interdigitating with those displayed from a similar alpha helix of a second polypeptide, facilitating dimerization.
(12 Dec 1998)
leucine-induced hypoglycaemia Rare cause of hypoglycaemia occurring following ingestion of leucine. Seen especially in infants.
(05 Mar 2000)
leucine-trna ligase <enzyme> An enzyme that activates leucine with its specific transfer RNA.
Chemical name: L-Leucine:tRNA(Leu) ligase (AMP-forming)
Registry number: EC 6.1.1.4
(12 Dec 1998)
leucinic <chemistry> Pertaining to, or designating, an acid obtained from leucin, and
Synonym: oxycaproic acid.
Source: Websters Dictionary
(01 Mar 1998)
leucinopine <biochemistry, cell biology> An analogue of nopaline found in crown gall tumours (induced by Agrobacterium tumefasciens) that do not synthesise octopine or nopaline.
(15 Oct 1997)
leucinosis A condition in which there is an abnormally large proportion of leucine in the tissues and body fluids.
(05 Mar 2000)
leucinuria The excretion of leucine in the urine.
(05 Mar 2000)
MeSH(Medical Subject Headings) ¸ÂÃã °Ë»ö (http://www.nlm.nih.gov) °á°ú : 5 ÆäÀÌÁö: 1
  • Leucine - »õâ An essential branched-chain amino acid important for hemoglobin formation.
    Synonyms : L-Leucine, Leucine, L-Isomer, L-Isomer Leucine, Leucine, L Isomer
  • Leucine Dehydrogenase - »õâ An octameric enzyme belonging to the superfamily of amino acid dehydrogenases. Leucine dehydrogenase catalyzes the reversible oxidative deamination of L-LEUCINE, to 4-methyl-2-oxopentanoate (2-ketoisocaproate) and AMMONIA, with the corresponding reduction of the cofactor NAD+.
    Synonyms : L-Leucine Dehydrogenase, Leucine (Branched-Chain Amino Acid) Dehydrogenase, Dehydrogenase, L-Leucine, Dehydrogenase, Leucine, L Leucine Dehydrogenase
  • Leucine Transaminase - »õâ A PYRIDOXAL PHOSPHATE containing enzyme that catalyzes the reversible transamination of branched-chain AMINO ACIDS to 2-OXOGLUTARATE.
    Synonyms : Leucine Aminotransferase, Leucine alpha Ketoglutarate Aminotransferase, Aminotransferase, Leucine, Transaminase, Leucine
  • Leucine Zippers - »õâ DNA-binding motifs formed from two alpha-helixes which intertwine for about eight turns into a coiled coil and then bifurcate to form Y shaped structures. Leucines occurring in heptad repeats end up on the same sides of the helixes and are adjacent to each other in the stem of the Y (the "zipper" region). The DNA-binding residues are located in the bifurcated region of the Y.
    Synonyms : Leucine Zipper, Zipper, Leucine, Zippers, Leucine
  • Leucine-Responsive Regulatory Protein - »õâ A LEUCINE and DNA-binding protein that is found primarily in BACTERIA and ARCHAEA. It regulates GENETIC TRANSCRIPTION involved in METABOLISM of AMINO ACIDS in response to the increased concentration of LEUCINE.
    Synonyms : Leucine Responsive Regulatory Protein
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  • Leucine aminopeptidase - serum - »õâ
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leucine a white crystalline amino acid occurring in proteins that is essential for nutrition; obtained by the hydrolysis of most dietary proteins
Ãâó: wordnet.princeton.edu/perl/webwn
leucine zipper A structural motif characteristic of DNA-binding proteins consisting of a protein dimer formed by two interacting a helices from separate proteins.
Ãâó: www.genpromag.com/Glossary~LETTER~L.html
leucine zipper Configuration of a DNA-binding protein in which leucine residues on two protein alpha-helices interdigitate in zipper fashion to stabilize the protein.
Ãâó: helios.bto.ed.ac.uk/bto/glossary/lm.htm
leucine zipper a protein domain that mediates dimer formation and is normally adjacent to a basic DNA-binding domain. It is characterized by a pattern of five leucine residues each separated by six residues.
Ãâó: www.oup.com/uk/booksites/content/0199264724/studen...
leucine (Leu): an aliphatic, nonpolar, neutral amino acid that, unlike most amino acids, is sparingly soluble in water chem phys
Ãâó: www.desicca.de/plant_breeding/Dictionary/Dictionar...
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leucin a white crystalline amino acid occurring in proteins that is essential for nutrition
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