GO:0004084 branched-chain-amino-acid:2-oxoglutarate transaminase activity: Mechanism, Genes and Research Methods
Research-grade guide for scientists and biopharma professionals
Key Takeaways
• GO:0004084 describes the reversible transamination of L-leucine, L-isoleucine and L-valine with 2-oxoglutarate to yield L-glutamate and the corresponding branched-chain 2-oxocarboxylates.
• The reaction is catalysed by branched-chain amino acid aminotransferases (BCATs), which are pyridoxal 5'-phosphate-dependent enzymes.
• BCAT activity is central to branched-chain amino acid (BCAA) catabolism and to the recycling of nitrogen via glutamate, and it is dysregulated in starvation, diabetes and acidosis.
• In cancer, BCAT1-mediated consumption of 2-oxoglutarate can restrict alpha-ketoglutarate availability and promote IDH-mutant-like DNA hypermethylation in leukaemia stem cells.
• Loss of BCAT activity or pharmacological elevation of 2-oxoglutarate can suppress lymphoma growth, linking this enzymatic activity to tumour metabolism.
• CRISPR knockout, point-mutation, knock-in and overexpression models are the main tools for testing causal roles of BCAT genes in metabolism and disease.
Description
GO:0004084, branched-chain-amino-acid:2-oxoglutarate transaminase activity, is a molecular function that catalyses the reversible transfer of an amino group from a branched-chain amino acid (L-leucine, L-isoleucine or L-valine) to 2-oxoglutarate, producing L-glutamate and the corresponding branched-chain 2-oxocarboxylate. This reaction is the first committed step in the catabolism of branched-chain amino acids (BCAAs) and is therefore a key node connecting amino acid breakdown, nitrogen handling and energy metabolism. The activity is carried out by branched-chain amino acid aminotransferases (BCATs), pyridoxal 5'-phosphate-dependent enzymes that have been purified and characterised from mammalian tissues and bacteria. Because BCAAs are elevated in starvation and diabetes, and because BCAT flux influences the availability of 2-oxoglutarate, this GO term is of interest to researchers in metabolism, cancer biology and nutrition. Understanding GO:0004084 helps explain how cells balance BCAA catabolism with glutamate and 2-oxoglutarate pools, and it provides a mechanistic entry point for studying metabolic disease and tumour metabolism.
branched-chain-amino-acid:2-oxoglutarate transaminase activity At A Glance
| GO ID | GO:0004084 |
|---|---|
| GO term | branched-chain-amino-acid:2-oxoglutarate transaminase activity |
| Ontology | molecular_function |
| Synonym | branched-chain amino acid aminotransferase activity; branched-chain aminotransferase activity; transaminase B activity; L-branched chain amino acid aminotransferase activity |
| Major function | Reversible transamination of L-leucine, L-isoleucine and L-valine with 2-oxoglutarate to form L-glutamate and branched-chain 2-oxocarboxylates |
| Cofactor | Pyridoxal 5'-phosphate-dependent enzyme activity |
| Substrates | L-leucine, L-isoleucine, L-valine and 2-oxoglutarate |
| Products | L-glutamate and a 2-oxocarboxylate derived from the branched-chain amino acid |
| Pathway context | First committed step of branched-chain amino acid catabolism |
What Is GO:0004084?
In simple terms, GO:0004084 is the enzyme activity that swaps an amino group from a branched-chain amino acid onto 2-oxoglutarate. The official definition states: Catalysis of the reaction: a branched-chain amino acid (L-leucine, L-isoleucine and L-valine) + 2-oxoglutarate = L-glutamate + a 2-oxocarboxylate derived from the branched-chain amino acid. This is a reversible transamination reaction that requires pyridoxal 5'-phosphate as a cofactor and is catalysed by branched-chain amino acid aminotransferases. The reaction is part of BCAA catabolism and links BCAA nitrogen to glutamate and the 2-oxoglutarate/glutamate pool.
Why Is branched-chain-amino-acid:2-oxoglutarate transaminase activity Important in Cell Biology?
GO:0004084 is important because it controls the first step of BCAA catabolism and directly influences the cellular pools of glutamate and 2-oxoglutarate, two metabolites with wide-ranging roles in nitrogen disposal, anaplerosis and epigenetic regulation. Dysregulation of this activity is observed in metabolic stress states such as starvation, diabetes and acidosis, where BCAA levels are altered. In cancer, BCAT1-mediated transamination can lower 2-oxoglutarate levels and contribute to a DNA hypermethylation phenotype in leukaemia stem cells, while promoting 2-oxoglutarate availability can suppress lymphoma growth. Therefore, measuring and manipulating GO:0004084 is central to understanding metabolic reprogramming in disease.
• It catalyses the first committed step of BCAA catabolism, determining how leucine, isoleucine and valine are funnelled into oxidative and anaplerotic pathways.
• It produces L-glutamate, a central nitrogen donor and neurotransmitter precursor, linking BCAA breakdown to nitrogen homeostasis.
• It consumes 2-oxoglutarate, a TCA cycle intermediate and cofactor for dioxygenases, thereby influencing epigenetic and metabolic signalling.
• BCAA levels are increased in starvation and diabetes, making this activity relevant to metabolic disease research.
• Altered BCAA metabolism in acidosis indicates that this activity is subject to physiological regulation in muscle.
• BCAT1 activity can restrict alpha-ketoglutarate levels in AML stem cells and promote IDH-mutant-like DNA hypermethylation.
• Elevating alpha-ketoglutarate can promote amino acid depletion and suppress B-cell lymphoma growth, highlighting the therapeutic relevance of this pathway.
• The enzyme is a validated target for biochemical and structural studies, with purification protocols established from mammalian and bacterial sources.
• Dietary BCAA antagonism studies in chicks show that this activity sits within a broader nutritional network of branched-chain amino acid balance.
• It provides a mechanistic link between amino acid metabolism, intestinal function and whole-body nitrogen economy.
Molecular Mechanism of branched-chain-amino-acid:2-oxoglutarate transaminase activity
Substrate recognition and binding
In simple terms: The enzyme first grabs a branched-chain amino acid and 2-oxoglutarate.
Branched-chain amino acid aminotransferases bind L-leucine, L-isoleucine or L-valine together with 2-oxoglutarate in a ternary complex. The enzyme active site accommodates the branched side chains of these amino acids, which distinguishes this activity from other aminotransferases. Purification studies from mouse testicular tissue and Helicobacter pylori have shown that the enzyme can act on all three BCAAs, consistent with the GO definition.
Pyridoxal 5'-phosphate-dependent catalysis
In simple terms: A vitamin B6-derived cofactor temporarily holds the amino group during the swap.
The transamination reaction proceeds through a ping-pong bi-bi mechanism in which pyridoxal 5'-phosphate (PLP) forms a Schiff base with the amino group of the branched-chain amino acid, generating a pyridoxamine intermediate and releasing the branched-chain 2-oxocarboxylate. The amino group is then transferred to 2-oxoglutarate to form L-glutamate and regenerate the PLP form of the enzyme. This PLP-dependent chemistry is a hallmark of aminotransferases and is required for GO:0004084 activity.
Reversibility and metabolic context
In simple terms: The reaction can run in either direction, depending on what the cell needs.
The transamination is reversible, so the enzyme can either degrade BCAAs to their 2-oxocarboxylates or synthesise BCAAs from those keto acids when glutamate is abundant. In muscle, BCAA metabolism is abnormally regulated in acidosis, indicating that the direction and flux through this activity respond to physiological pH and hormonal signals. This reversibility allows the reaction to buffer nitrogen and carbon flux between BCAAs, glutamate and 2-oxoglutarate.
Role in 2-oxoglutarate and glutamate pools
In simple terms: By consuming 2-oxoglutarate and making glutamate, the enzyme changes the cell's metabolite balance.
Because the reaction consumes 2-oxoglutarate and produces L-glutamate, it directly influences the availability of alpha-ketoglutarate for other processes. In AML stem cells, BCAT1 restricts alpha-ketoglutarate levels, leading to an IDH-mutant-like DNA hypermethylation pattern. Conversely, increasing alpha-ketoglutarate can drive amino acid depletion and suppress B-cell lymphoma growth, showing that the balance of this reaction has functional consequences for tumour cells. The reaction also connects to intestinal function, where alpha-ketoglutarate and BCAA metabolism support nitrogen handling.
Nutritional and physiological regulation
In simple terms: Diet and whole-body physiology can change how active this pathway is.
Dietary branched-chain amino acid antagonism in chicks alters growth and amino acid balance, indicating that the transamination step is sensitive to the dietary BCAA profile. In starvation and diabetes, BCAAs accumulate, which implies that flux through GO:0004084 and downstream catabolic steps is altered. These observations place the enzyme within a broader regulatory network that includes substrate supply, hormone signalling and acid-base status.
Key Genes Involved in GO:0004084 branched-chain-amino-acid:2-oxoglutarate transaminase activity
The genes below encode the enzymes, transporters and regulatory proteins most directly associated with branched-chain-amino-acid:2-oxoglutarate transaminase activity and its metabolic context.
| Gene | Major Role | Research Relevance |
|---|---|---|
| BCAT1 | Cytosolic branched-chain amino acid aminotransferase that catalyses GO:0004084 | Restricts alpha-ketoglutarate in AML stem cells and promotes hypermethylation |
| BCAT2 | Mitochondrial branched-chain amino acid aminotransferase that catalyses GO:0004084 | Central to BCAA catabolism and mitochondrial nitrogen handling |
| BCKDHA | Component of the branched-chain alpha-ketoacid dehydrogenase complex downstream of BCAT | Links BCAT flux to BCAA oxidation |
| BCKDHB | Component of the branched-chain alpha-ketoacid dehydrogenase complex | Downstream of GO:0004084 in BCAA catabolism |
| DBT | Dihydrolipoamide branched chain transacylase in the BCKDH complex | Downstream enzyme in BCAA catabolism |
| DLD | Dihydrolipoamide dehydrogenase shared with pyruvate and alpha-ketoglutarate dehydrogenases | Connects BCAA catabolism to mitochondrial redox |
| SLC7A5 | Large neutral amino acid transporter that imports BCAAs | Controls substrate supply for BCAT activity |
| SLC3A2 | Heavy chain partner of amino acid transporters | Supports BCAA uptake and mTOR signalling |
| SLC1A5 | Glutamine transporter that feeds glutamate and 2-oxoglutarate pools | Indirectly supplies substrates for transamination |
| GLS | Glutaminase that generates glutamate from glutamine | Provides glutamate for BCAA synthesis and nitrogen exchange |
| GLUD1 | Glutamate dehydrogenase that interconverts glutamate and 2-oxoglutarate | Links GO:0004084 to TCA cycle anaplerosis |
| IDH1 | Isocitrate dehydrogenase producing alpha-ketoglutarate in the cytosol | Mutant IDH1 produces 2-hydroxyglutarate and interacts with BCAT-driven methylation phenotypes |
| IDH2 | Mitochondrial isocitrate dehydrogenase producing alpha-ketoglutarate | Relevant to alpha-ketoglutarate-dependent processes affected by BCAT |
| TET2 | Alpha-ketoglutarate-dependent DNA demethylase | Sensitive to alpha-ketoglutarate levels influenced by BCAT1 |
| KDM4A | Alpha-ketoglutarate-dependent histone demethylase | Epigenetic reader of alpha-ketoglutarate availability |
| MYC | Oncogenic transcription factor that can drive metabolic reprogramming | Context for BCAA metabolism in cancer |
| mTOR | Kinase complex that senses amino acids including leucine | Connects BCAA levels to growth signalling |
| GCN2 | Amino acid sensor kinase activated by amino acid depletion | Responds to altered BCAA availability |
How Is branched-chain-amino-acid:2-oxoglutarate transaminase activity Regulated?
GO:0004084 is regulated at multiple levels. Substrate availability of BCAAs and 2-oxoglutarate directly determines flux through the reaction, and BCAA levels rise in starvation and diabetes, indicating that whole-body metabolic state influences this activity. In muscle, BCAA metabolism is abnormally regulated in acidosis, showing that pH and hormonal context can alter the pathway. Downstream, the branched-chain alpha-ketoacid dehydrogenase complex controls BCAA oxidation and is subject to phosphorylation-based regulation, which indirectly affects BCAT flux. Amino acid sensing pathways such as mTOR and GCN2 respond to BCAA availability and can feed back on metabolism, linking GO:0004084 to growth and stress signalling. In cancer, oncogenic programmes can alter BCAT1 expression and alpha-ketoglutarate levels, further modulating the effective activity of this enzyme.
branched-chain-amino-acid:2-oxoglutarate transaminase activity and Human Disease
| Gene | Disease / Biology | Potential Experimental Model |
|---|---|---|
| BCAT1 | AML stem cell maintenance and DNA hypermethylation | BCAT1 knockout and overexpression in leukaemia cell lines |
| BCAT1 | B-cell lymphoma growth suppression by alpha-ketoglutarate | BCAT1 knockout lymphoma cells treated with alpha-ketoglutarate |
| BCAT2 | BCAA catabolism in metabolic stress | BCAT2 knockout hepatocytes or myotubes |
| BCKDHA | Branched-chain ketoacid dehydrogenase deficiency (maple syrup urine disease) | Point-mutation knock-in models of BCKDH complex |
| SLC7A5 | BCAA uptake and mTOR signalling | SLC7A5 knockout cells with BCAA tracing |
Cancer metabolism and epigenetic reprogramming
BCAT1-mediated transamination restricts alpha-ketoglutarate levels in AML stem cells, leading to an IDH-mutant-like DNA hypermethylation phenotype that supports leukaemic stemness. In B-cell lymphoma, increasing alpha-ketoglutarate promotes amino acid depletion and suppresses tumour growth and development, indicating that the balance of this reaction is therapeutically relevant. These findings link GO:0004084 to epigenetic regulation and tumour metabolism.
Metabolic stress: starvation, diabetes and acidosis
Branched-chain amino acids are increased in starvation and diabetes, which implies altered flux through BCAA catabolism and GO:0004084. In rat muscle, BCAA metabolism is abnormally regulated in acidosis, suggesting that acid-base disturbances change the pathway. These conditions are relevant to understanding how BCAA transamination contributes to metabolic disease.
Nutritional and intestinal biology
Dietary branched-chain amino acid antagonism in chicks affects growth and amino acid balance, showing that the transamination step is sensitive to nutritional input. Alpha-ketoglutarate and intestinal function are also linked, with alpha-ketoglutarate supporting nitrogen handling and intestinal metabolism. This places GO:0004084 in the context of nutrition and gut physiology.
From branched-chain-amino-acid:2-oxoglutarate transaminase activity-Related Genes to Experimental Models
| Research Question | Suitable Model |
|---|---|
| Does BCAT1 loss alter alpha-ketoglutarate levels and DNA methylation? | BCAT1 knockout in AML cell lines |
| Does increasing alpha-ketoglutarate suppress lymphoma growth? | BCAT1 knockout or overexpression lymphoma models with alpha-ketoglutarate treatment |
| How does acidosis change BCAA transamination flux? | BCAT2 point-mutation or knockout muscle cells under acidic conditions |
| What is the effect of BCAA antagonism on growth? | Dietary BCAA manipulation in chick models |
| Can BCAT activity be measured in tissue extracts? | Purified enzyme assays from mouse testis or H. pylori |
| Does BCAT1 overexpression drive epigenetic changes? | BCAT1 overexpression in leukaemia or lymphoma cells |
How to Study the branched-chain-amino-acid:2-oxoglutarate transaminase activity Process
| Method | What It Measures | Typical Application |
|---|---|---|
| Enzyme activity assay | Transamination of BCAAs with 2-oxoglutarate | Biochemical characterisation of BCAT enzymes |
| Metabolomics | BCAA, glutamate and 2-oxoglutarate levels | Metabolic phenotyping of BCAT mutants |
| Stable isotope tracing | Flux through BCAA catabolism | Determining direction and rate of GO:0004084 |
| DNA methylation profiling | Global and locus-specific 5-methylcytosine | Assessing alpha-ketoglutarate-dependent hypermethylation |
| Histone methylation profiling | Methyl marks on histones | Linking BCAT activity to epigenetic state |
| CRISPR knockout | Loss-of-function phenotype | Testing causal role of BCAT1 or BCAT2 |
| Overexpression | Gain-of-function phenotype | Testing whether increased BCAT activity drives metabolic changes |
| Cell growth assays | Proliferation and viability | Evaluating therapeutic relevance of BCAT inhibition |
Enzymatic activity assays
Direct measurement of GO:0004084 uses purified enzyme or tissue extracts incubated with a branched-chain amino acid and 2-oxoglutarate, followed by detection of L-glutamate or the branched-chain 2-oxocarboxylate. Purification protocols from mouse testicular tissue and Helicobacter pylori provide validated starting points for biochemical assays.
Metabolomics and stable isotope tracing
Metabolomics can quantify BCAAs, glutamate and 2-oxoglutarate, while stable isotope tracing with labelled leucine, isoleucine or valine can measure flux through the transamination step. Such approaches have been used to link BCAT1 activity to alpha-ketoglutarate restriction and hypermethylation in AML and to alpha-ketoglutarate-mediated lymphoma suppression.
Epigenomic profiling
Because BCAT1 can restrict alpha-ketoglutarate and produce an IDH-mutant-like DNA hypermethylation pattern, DNA methylation arrays or bisulfite sequencing are useful readouts for the downstream consequences of GO:0004084 activity. Histone methylation profiling can also report on alpha-ketoglutarate-dependent demethylase activity.
Genetic and pharmacological perturbation
CRISPR knockout, point-mutation, knock-in and overexpression models allow causal testing of BCAT genes. Combining these models with alpha-ketoglutarate supplementation or BCAA restriction helps dissect how GO:0004084 influences cell growth and metabolism.
How CRISPR Can Be Used to Study GO:0004084 branched-chain-amino-acid:2-oxoglutarate transaminase activity
Knockout
CRISPR knockout of BCAT1 or BCAT2 eliminates GO:0004084 activity in the targeted compartment, allowing researchers to test whether loss of transamination alters alpha-ketoglutarate levels, DNA methylation and cell growth. BCAT1 knockout has been used to show that BCAT1 restricts alpha-ketoglutarate in AML stem cells, and loss of BCAT activity can sensitise lymphoma cells to alpha-ketoglutarate-mediated suppression.
Point Mutation
Point mutations in the catalytic site or cofactor-binding residues of BCAT enzymes can dissociate enzymatic activity from other functions. Such models are useful for testing whether the transamination reaction itself, rather than a scaffolding role, is responsible for observed phenotypes.
Knock-in
Knock-in of tagged or reporter alleles at the BCAT1 or BCAT2 locus enables tracking of enzyme expression, localisation and interaction partners in cells and tissues. This is valuable for linking GO:0004084 activity to specific subcellular compartments and metabolic states.
Overexpression
Overexpression of BCAT1 or BCAT2 increases transamination capacity and can drive alpha-ketoglutarate depletion, epigenetic changes and altered growth. Overexpression models complement knockout studies by testing sufficiency of the activity in metabolic reprogramming.
How EDITGENE Supports branched-chain-amino-acid:2-oxoglutarate transaminase activity Research
Researchers studying branched-chain-amino-acid:2-oxoglutarate transaminase activity-related genes often need to determine whether a candidate gene is causally involved in a metabolic or disease phenotype, and CRISPR-based models provide a direct way to test this. EDITGENE supports these studies with custom cell model generation and screening services tailored to BCAA metabolism and related pathways.
Contact EDITGENE today to design your custom CRISPR model for branched-chain-amino-acid:2-oxoglutarate transaminase activity research.
Related Products
| Product name | Cat.No. | Species | Gene ID | |
|---|---|---|---|---|
| BCAT1 Knockout HEK293 Cell Line | EDJ-KQ3038 | Human | 586 | Details Get a Quote |
| BCAT2 Knockout HEK293 Cell Line | EDJ-KQ4126 | Human | 587 | Details Get a Quote |
| BCAT1 Knockout A-549 Cell Line | EDJ-KQ24271 | Human | 586 | Details Get a Quote |
| BCAT1 Knockout HeLa Cell Line | EDJ-KQ24272 | Human | 586 | Details Get a Quote |
| BCAT2 Knockout A-549 Cell Line | EDJ-KQ26533 | Human | 587 | Details Get a Quote |
| BCAT2 Knockout HCT 116 Cell Line | EDJ-KQ26534 | Human | 587 | Details Get a Quote |
| BCAT2 Knockout HeLa Cell Line | EDJ-KQ26535 | Human | 587 | Details Get a Quote |
| BCAT1 Knockout Hep-G2 Cell Line | EDJ-KZ115 | Human | 586 | Details Get a Quote |
| BCAT1 Knockout Huh-7 Cell Line | EDJ-KZ116 | Human | 586 | Details Get a Quote |
| BCAT1 Knockout HCT 116 Cell Line | EDJ-KQ69670 | Human | 586 | Details Get a Quote |
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Frequently Asked Questions About branched-chain-amino-acid:2-oxoglutarate transaminase activity
What is GO:0004084?
GO:0004084 is the molecular function branched-chain-amino-acid:2-oxoglutarate transaminase activity, which catalyses the reversible transfer of an amino group from L-leucine, L-isoleucine or L-valine to 2-oxoglutarate, producing L-glutamate and a branched-chain 2-oxocarboxylate.
What does branched-chain-amino-acid:2-oxoglutarate transaminase activity do?
It performs the first committed step of branched-chain amino acid catabolism, using pyridoxal 5'-phosphate to transfer nitrogen from BCAAs to 2-oxoglutarate and generate glutamate.
Which genes encode branched-chain-amino-acid:2-oxoglutarate transaminase activity?
The activity is encoded by BCAT1 (cytosolic) and BCAT2 (mitochondrial) in mammals, with bacterial orthologues also characterised.
What diseases are linked to BCAT1 and BCAT2?
BCAT1 has been linked to AML stem cell maintenance and DNA hypermethylation, and to B-cell lymphoma growth suppression by alpha-ketoglutarate. BCAA metabolism is also altered in starvation, diabetes and acidosis.
How is branched-chain-amino-acid:2-oxoglutarate transaminase activity measured?
It is measured by enzyme assays detecting glutamate or branched-chain 2-oxocarboxylate formation, often combined with metabolomics and stable isotope tracing.
Why are BCAAs increased in starvation and diabetes?
BCAA levels rise in starvation and diabetes, indicating altered flux through BCAA catabolism that includes the transamination step catalysed by GO:0004084.
Does BCAT1 affect DNA methylation?
Yes, BCAT1 restricts alpha-ketoglutarate levels in AML stem cells, leading to an IDH-mutant-like DNA hypermethylation pattern.
Can alpha-ketoglutarate suppress lymphoma growth?
Studies show that alpha-ketoglutarate promotes amino acid depletion and suppresses B-cell lymphoma growth and development, linking the metabolite balance around GO:0004084 to tumour suppression.
What cofactor is required for GO:0004084?
The reaction requires pyridoxal 5'-phosphate, a vitamin B6-derived cofactor typical of aminotransferases.
How can CRISPR help study branched-chain-amino-acid:2-oxoglutarate transaminase activity?
CRISPR knockout, point-mutation, knock-in and overexpression models allow causal testing of BCAT genes and their effects on metabolism, epigenetics and disease phenotypes.
Conclusion
GO:0004084, branched-chain-amino-acid:2-oxoglutarate transaminase activity, is a central enzymatic function in BCAA catabolism that links amino acid breakdown to glutamate and 2-oxoglutarate pools. Its dysregulation is relevant to metabolic stress, cancer metabolism and epigenetic reprogramming, as shown by studies in AML and lymphoma. Continued research using CRISPR models and metabolic profiling will clarify how this activity contributes to health and disease.
References
- 1. Holeček M. 2020. Why Are Branched-Chain Amino Acids Increased in Starvation and Diabetes?. Nutrients 12(10) PMID: 33050579
- 2. Montamat EE et al.. 1978. Branched-chain amino acid aminotransferase in mouse testicular tissue.. J Reprod Fertil 53(1):117-23 PMID: 641889
- 3. Saito M et al.. 2007. Purification of branched-chain amino acid aminotransferase from Helicobacter pylori NCTC 11637.. Amino Acids 33(3):445-9 PMID: 17077963
- 4. Raffel S et al.. 2017. BCAT1 restricts αKG levels in AML stem cells leading to IDHmut-like DNA hypermethylation.. Nature 551(7680):384-388 PMID: 29144447
- 5. Jaafar C et al.. 2025. α-Ketoglutarate promotes amino acid depletion and suppresses B-cell lymphoma growth and development.. Blood 146(18):2217-2228 PMID: 40700634
- 6. Hou Y et al.. 2011. Alpha-Ketoglutarate and intestinal function.. Front Biosci (Landmark Ed) 16(3):1186-96 PMID: 21196226
- 7. Smith TK et al.. 1978. The branched-chain amino acid antagonism in chicks.. J Nutr 108(7):1180-91 PMID: 660310
- 8. May RC et al.. 1987. Branched-chain amino acid metabolism in rat muscle: abnormal regulation in acidosis.. Am J Physiol 252(6 Pt 1):E712-8 PMID: 3591935
