Related Experiment Video
Updated: Aug 6, 2026
09:27
Functional Complementation Analysis (FCA): A Laboratory Exercise Designed and Implemented to Supplement the Teaching of Biochemical Pathways
Published on: June 24, 2016
Structure and function of branched chain aminotransferases
1Department of Biochemistry, Wake Forest University School of Medicine, Winston-Salem, North Carolina 27157, USA.
Progress in Nucleic Acid Research and Molecular Biology
|October 20, 2001
Summary
Branched-chain aminotransferases (BCATs) are enzymes crucial for amino acid metabolism. Their unique structure and function are key to understanding neurodegenerative disorders and designing new therapies.
Area of Science:
- Biochemistry
- Enymology
- Neuroscience
Background:
- Branched-chain aminotransferases (BCATs) are pyridoxal phosphate (PLP)-dependent enzymes catalyzing BCAA metabolism.
- BCATs are structurally distinct, belonging to a novel protein fold (type IV), differing from other PLP enzyme classes.
- Eukaryotes possess mitochondrial (BCATm) and cytosolic (BCATc) isoforms, with distinct tissue distributions and roles.
Purpose of the Study:
- To elucidate the structural and functional characteristics of BCAT enzymes.
- To highlight the significance of BCATc in the central nervous system (CNS) and its role in neurotransmitter synthesis.
- To explore the therapeutic potential of targeting BCATs for neurodegenerative disorders.
Main Methods:
- Structural analysis of BCATs, including crystal structures.
- Comparative analysis with other PLP-dependent enzymes.
- Investigation of BCATm and BCATc roles in mammalian metabolism and the CNS.
Main Results:
- BCATs exhibit a unique fold (type IV) distinct from other PLP enzyme families.
- Catalysis occurs on the re face of the PLP cofactor, a characteristic of this enzyme class.
- BCATc is implicated in glutamate synthesis in the CNS and is a target for gabapentin.
Conclusions:
- BCATs represent a distinct enzyme family with unique structural and catalytic properties.
- BCATc plays a critical role in CNS function and glutamate metabolism.
- Structural insights into BCATs may pave the way for novel therapeutic strategies for neurodegenerative diseases.
More Related Videos
11:27X-Ray Crystallography to Study the Oligomeric State Transition of the Thermotoga maritima M42 Aminopeptidase TmPep1050
Published on: May 13, 2020
12:07Chemical Modification of the Tryptophan Residue in a Recombinant Ca2+-ATPase N-domain for Studying Tryptophan-ANS FRET
Published on: October 9, 2021
Related Concept Videos
02:26tRNA Activation
Aminoacyl-tRNA synthetases are present in both eukaryotes and bacteria. Though eukaryotes have 20 different aminoacyl-tRNA synthetases to couple to 20 amino acids, many bacteria do not have genes for all of these aminoacyl-tRNA synthetases. Despite this, they still use all 20 amino acids to synthesize their proteins. For instance, some bacteria do not have the gene encoding the enzyme that couples glutamine with its partner tRNA. In these organisms, one enzyme adds glutamic acid to all of the...
01:48ATP Synthase: Mechanism
In animals, the mitochondrial F1F0 ATP synthase is the key protein that synthesizes ATP molecules through a complex catalytic mechanism. While the nuclear genome encodes the majority of ATP synthase subunits, the mitochondrial genome encodes some of the enzyme's most critical components. The formation of this multi-subunit enzyme is a complex multi-step process regulated at the level of transcription, translation, and assembly. Defects in one or more of these steps can result in decreased ATP...
01:18ATP Synthase: Structure
ATP synthase or ATPase is among the most conserved proteins found in bacteria, mammals, and plants. This enzyme can catalyze a forward reaction in response to the electrochemical gradient, producing ATP from ADP and inorganic phosphate. ATP synthase can also work in a reverse direction by hydrolyzing ATP and generating an electrochemical gradient. Different forms of ATP synthases have evolved special features to meet the specific demands of the cell. Based on their specific feature, ATP...
01:19Allosteric Proteins-ATCase
Binding sites linkages can regulate a protein's function. For example, enzyme activity is often regulated through a feedback mechanism where the end product of the biochemical process serves as an inhibitor.
Aspartate transcarbamoylase (ATCase) is a cytosolic enzyme that catalyzes the condensation of L-aspartate and carbamoyl phosphate to N-carbamoyl-L-aspartate. This reaction is the first step in pyrimidine biosynthesis. UTP and CTP, the end products of the pyrimidine synthesis pathway,...
Aspartate transcarbamoylase (ATCase) is a cytosolic enzyme that catalyzes the condensation of L-aspartate and carbamoyl phosphate to N-carbamoyl-L-aspartate. This reaction is the first step in pyrimidine biosynthesis. UTP and CTP, the end products of the pyrimidine synthesis pathway,...
02:26tRNA Activation
Aminoacyl-tRNA synthetases are present in both eukaryotes and bacteria. Though eukaryotes have 20 different aminoacyl-tRNA synthetases to couple to 20 amino acids, many bacteria do not have genes for all of these aminoacyl-tRNA synthetases. Despite this, they still use all 20 amino acids to synthesize their proteins. For instance, some bacteria do not have the gene encoding the enzyme that couples glutamine with its partner tRNA. In these organisms, one enzyme adds glutamic acid to all of the...
01:29Amino Acid Biosynthetic Pathways
Amino acid biosynthesis is essential for cell growth, protein synthesis, and metabolic regulation. Cells generate essential and non-essential amino acids from metabolic intermediates to sustain vital biological functions. These intermediates originate from key metabolic pathways: glycolysis, the tricarboxylic acid (TCA) cycle, and the pentose phosphate pathway. Important precursors include α-ketoglutarate, pyruvate, oxaloacetate, phosphoenolpyruvate, and erythrose-4-phosphate, which provide...