Display Settings:


Send to:

Choose Destination

L-alanine degradation III

In eukaryotes, L-alanine is degraded through transamination to pyruvate by alanine aminotransferase. Pyruvate is transported into the mitochondrion where it is oxidatively decarboxylated by the pyruvate dehydrogenase complex to carbon dioxide and acetyl-CoA (as shown in the pathway link). Acetyl-CoA enters the TCA cycle . Biosynthetically, pyruvate is involved in gluconeogenesis (see MetaCyc pathway |FRAME: GLUCONEO-PWY|) and is also a precursor of the pyruvate family of amino acids: alanine, valine, leucine and isoleucine. In plants and bacteria, it is also a precursor of isoprenoids (see MetaCyc pathway |FRAME: NONMEVIPP-PWY|). Alanine aminotransferase is a commonly used diagnostic marker in humans. It is produced mainly in the liver and its presence in serum is an indicator of liver disease |CITS: [1992953]|. The enzyme is present as isozymes in both the cytosol and mitochondrion. Expression of the isozymes varies among tissues and is species-specific (in |CITS: [16495081]|). In bacteria, alanine is converted to pyruvate by oxidative deamination (|CITS: [Gottschalk1986]|) (see MetaCyc pathway |FRAME: PWY1-2|). An alanine aminotransferase has been identified in the archaeon |FRAME:TAX-2261| and is thought to function biosynthetically, transaminating pyruvate with glutamate |CITS: [10762259]| (see MetaCyc pathway |FRAME: PWY-5096|.

from BIOCYC source record: META_ALANINE-DEG3-PWY
Type: pathway
Taxonomic scope
conserved biosystem

Supplemental Content

Recent activity

Your browsing activity is empty.

Activity recording is turned off.

Turn recording back on

See more...
Support Center