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Contents 1 Aspartate Aminotransferase 1.1 General Information 1.2 Structure 1.3 Function 1.4 Clinical Applications 1.5 Additional Resources 1.6 References

Aspartate Aminotransferase

This Sandbox is Reserved from January 10, 2010, through April 10, 2011 for use in BCMB 307-Proteins course taught by Andrea Gorrell at the University of Northern British Columbia, Prince George, BC, Canada.

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spinqualitylabelsall models PDB ID 1b4x Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image
1b4x, resolution 2.45Å ()
Ligands:	,
Activity:	Aspartate transaminase, with EC number 2.6.1.1
Structural annotation: Resources: CATH : 1B4Xa01, 1B4Xa02 InterPro : Ipr000796, Ipr004839, Ipr015421, Ipr015424, Ipr004838 Pfam : PF00155 SCOP : d1b4xa_ UniProt : P00509
Functional annotation: Cellular component: cytoplasm Biological process: biosynthetic process amino acid metabolic process Molecular function: pyridoxal phosphate binding catalytic activity transferase activity, transferring nitrogenous groups aspartate transaminase activity transaminase activity protein binding transferase activity
Evolutionary conservation: Toggle Conservation Colors: Rows = identical sequences: Further Information: Caveats, Explanation, Complete Results at ConSurfDB
Resources:	FirstGlance, OCA, PDBsum, RCSB
Coordinates:	save as pdb, mmCIF, xml

General Information

Aspartate Aminotransferase (AST), also know as Glutamic aspartic transaminase, glutamic oxaloacetic transaminase, and transaminase A., is an enzyme that is a member of the class-I pyridoxal-phosphate-dependent aminotransferase family.It is coded by the gene GOT1. It is a homodimer that is 413 amino acids long and serves a critical role in amino acid metabolism. Within prokaryote cells it is exclusively found in the cytosol, but in eukaryotic cells there are cytosol, mitochondrial, and chloroplast isozymes. 

In the human body it is produced by the brain, skeletal muscles, liver, pancreas, red blood cells, and kidneys. The wide range of tissues in which it is made, separates it from the similar enzyme alanine transaminase (ALT) which is found primarily in the liver.

Structure

Function

Clinical Applications

Additional Resources

References