Search results
Results from the WOW.Com Content Network
Leucine ball and stick model spinning. Leucine (symbol Leu or L) [3] is an essential amino acid that is used in the biosynthesis of proteins.Leucine is an α-amino acid, meaning it contains an α-amino group (which is in the protonated −NH 3 + form under biological conditions), an α-carboxylic acid group (which is in the deprotonated −COO − form under biological conditions), and a side ...
Download QR code; Print/export ... Download as PDF; Printable version; In other projects Wikidata item ... The complete data for Leucine. General information ...
The enzyme contains α and β subunits. Human MCCCα is composed of 725 amino acids which harbor a covalently bound biotin essential for the ATP-dependent carboxylation; MCCCβ has 563 amino acids that possess carboxyltransferase activity which presumably is essential for binding to 3-methylcrotonyl CoA. [5]
To transclude this template as is, use: {{Leucine metabolism in humans | note=yes}} Important: If the note parameter is set to yes (|note=yes), the article receiving the transclusion from this template must have a reference group for "note" included in a "Notes" or "References" section at the end of the article (code: {{Reflist|group=note}}).
The leucines are primarily the four isomeric amino acids: leucine, isoleucine, tert-leucine (terleucine, pseudoleucine) and norleucine. [1] Being compared with the four butanols, they could be classified as butyl-substituted glycines; they represent all four possible variations.
Summary of amino acid catabolism. A ketogenic amino acid is an amino acid that can be degraded directly into acetyl-CoA, which is the precursor of ketone bodies and myelin, particularly during early childhood, when the developing brain requires high rates of myelin synthesis. [1]
Leucine is an essential amino acid, and its degradation is critical for many biological duties. [ 3 ] α-KIC is produced in one of the first steps of the pathway by branched-chain amino acid aminotransferase by transferring the amine on L-leucine onto alpha ketoglutarate , and replacing that amine with a ketone .
Transamination is mediated by several types of aminotransferase enzymes. An aminotransferase may be specific for an individual amino acid, or it may be able to process any member of a group of similar ones, for example the branched-chain amino acids, which comprises valine, isoleucine, and leucine.