GO:0070279 vitamin B6 binding: Mechanism, Genes and Research Methods
Research-grade guide for scientists and biopharma professionals
Key Takeaways
• GO:0070279 (vitamin B6 binding) is a molecular_function term describing binding to pyridoxal, pyridoxamine, pyridoxine, or the active coenzyme pyridoxal phosphate (PLP).
• PLP is the catalytically active form of vitamin B6 and binds within the active site of enzymes such as aspartate transaminase, where its binding and reaction chemistry have been studied for decades.
• The conserved PLP-binding protein YggS/PLPBP is a key regulator of vitamin B6 and amino acid homeostasis, illustrating that vitamin B6 binding is not limited to classical enzymes.
• Vitamin B6 binding and availability influence diverse biology, including CD8+ T cell stemness and antitumor function, acute myeloid leukemia vitamin B6 addiction, and modulation of DNA-binding protein activity.
• Vitamin B6 status also interacts with drugs and with antibiotic resensitization of mcr-carrying Gram-negative bacteria, and vitamin B6-based metal complexes can act as DNA/BSA-binding agents inducing apoptosis in hepatocarcinoma cells.
• Studying vitamin B6 binding requires combining structural, biochemical, and CRISPR-based functional approaches to distinguish binding events from downstream metabolic consequences.
Description
GO:0070279, vitamin B6 binding, is a Gene Ontology molecular_function term defined as binding to a vitamin B6 compound: pyridoxal, pyridoxamine, pyridoxine, or the active form, pyridoxal phosphate. Vitamin B6 compounds are small pyridine derivatives that serve as essential cofactors and signaling molecules in all domains of life, and their binding to proteins underlies a wide range of enzymatic and regulatory functions. The term is therefore central to understanding how cells sense, utilize, and respond to vitamin B6. For researchers, GO:0070279 provides a precise annotation target for proteins that physically interact with vitamin B6 compounds, distinguishing them from proteins involved in vitamin B6 transport, synthesis, or downstream metabolism. Classic work on aspartate transaminase established the principles of PLP binding and reaction chemistry within a catalytic center, showing that the coenzyme forms a Schiff base with a conserved lysine and participates directly in transamination. More recent studies have expanded the biological scope of vitamin B6 binding: the conserved PLP-binding protein YggS/PLPBP regulates vitamin B6 and amino acid homeostasis, vitamin B6 preserves stemness-like phenotypes and antitumor ability of CD8+ T cells, and vitamin B6 addiction has been described in acute myeloid leukemia. Vitamin B6 binding also intersects with pharmacology and infectious disease, as drug-vitamin B6 interactions are well documented and vitamin B6 can resensitize mcr-carrying Gram-negative bacteria to colistin. Understanding GO:0070279 thus connects fundamental enzymology to immunology, oncology, and antimicrobial research.
vitamin B6 binding At A Glance
| GO ID | GO:0070279 |
|---|---|
| GO term | vitamin B6 binding |
| Ontology | molecular_function |
| Synonym | none |
| Definition | Binding to a vitamin B6 compound: pyridoxal, pyridoxamine, pyridoxine, or the active form, pyridoxal phosphate. |
| Major function | Physical interaction with vitamin B6 compounds, enabling cofactor-dependent catalysis, regulation, or sensing. |
| Active coenzyme form | Pyridoxal phosphate (PLP). |
| Representative protein | YggS/PLPBP, a conserved PLP-binding protein involved in vitamin B6 and amino acid homeostasis. |
| Disease relevance | Cancer (acute myeloid leukemia, hepatocellular carcinoma), immune regulation, and antimicrobial resistance. |
What Is GO:0070279?
In your own words, GO:0070279 (vitamin B6 binding) describes the molecular function of selectively interacting with any vitamin B6 compound, including pyridoxal, pyridoxamine, pyridoxine, and the active coenzyme pyridoxal phosphate (PLP). This binding can be non-covalent or, in the case of PLP-dependent enzymes, can involve formation of a covalent Schiff base intermediate with a catalytic lysine residue. The term is agnostic to the downstream consequence of binding: a protein annotated with GO:0070279 may use the bound vitamin B6 compound as a cofactor for catalysis, as a regulatory ligand, or as a substrate for further chemistry. It is distinct from terms describing vitamin B6 transport, biosynthesis, or catabolism, because it specifically captures the physical interaction between a protein and a vitamin B6 molecule.
Why Is vitamin B6 binding Important in Cell Biology?
Vitamin B6 binding is important because it governs the function of enzymes and regulatory proteins that control amino acid metabolism, neurotransmitter synthesis, immune cell function, and redox biology. PLP, the active form of vitamin B6, is one of the most versatile coenzymes in nature, and its binding within active sites determines catalytic specificity and reactivity. Beyond classical enzymology, vitamin B6 binding proteins such as YggS/PLPBP act as homeostatic regulators, linking vitamin B6 availability to amino acid balance. In immunology, vitamin B6 preserves stemness-like phenotypes and antitumor ability of CD8+ T cells, indicating that vitamin B6 binding and metabolism are required for effective T cell responses. In oncology, acute myeloid leukemia can exhibit vitamin B6 addiction, making vitamin B6 binding pathways potential therapeutic vulnerabilities. Vitamin B6 also modulates gene expression by inactivating tissue-specific DNA-binding proteins, and drug-vitamin B6 interactions can alter drug efficacy or toxicity. Finally, vitamin B6 can resensitize mcr-carrying Gram-negative bacteria to colistin, connecting vitamin B6 binding and metabolism to antimicrobial resistance.
• PLP binding is essential for the catalytic activity of transaminases and many other enzymes, as established for aspartate transaminase.
• YggS/PLPBP is a conserved PLP-binding protein that regulates vitamin B6 and amino acid homeostasis.
• Vitamin B6 preserves stemness-like phenotypes and antitumor ability of CD8+ T cells, linking vitamin B6 binding to immune function.
• Acute myeloid leukemia can show vitamin B6 addiction, suggesting vitamin B6 binding pathways as therapeutic targets.
• Vitamin B6 modulates expression of the albumin gene by inactivating a tissue-specific DNA-binding protein in rat liver.
• Drug-vitamin B6 interactions can affect drug pharmacokinetics and vitamin B6 status.
• Vitamin B6 resensitizes mcr-carrying Gram-negative bacteria to colistin, linking vitamin B6 to antimicrobial resistance.
• Metal complexes containing vitamin B6-based scaffolds can act as DNA/BSA-binding agents and induce apoptosis in hepatocarcinoma (HepG2) cells.
• Vitamin B6 binding is distinct from transport and synthesis, making GO:0070279 a precise annotation for functional studies.
• Understanding vitamin B6 binding supports research in enzymology, immunology, oncology, and infectious disease.
What Happens During vitamin B6 binding?
Recognition and initial binding of vitamin B6 compounds
In simple terms: First, the protein recognizes and grabs the vitamin B6 molecule.
Vitamin B6 binding begins with molecular recognition of pyridoxal, pyridoxamine, pyridoxine, or PLP by a protein binding pocket. In PLP-dependent enzymes such as aspartate transaminase, the coenzyme is bound within the catalytic center, where specific residues position the pyridine ring and phosphate group for subsequent chemistry. The conserved PLP-binding protein YggS/PLPBP also binds PLP, and this binding is linked to vitamin B6 and amino acid homeostasis. The initial binding event is non-covalent and reversible, allowing the protein to sample and retain the vitamin B6 compound.
Schiff base formation and catalytic activation
In simple terms: The vitamin B6 molecule then forms a temporary chemical link with the protein to become active.
For PLP-dependent enzymes, binding is followed by formation of a Schiff base between the aldehyde group of PLP and the epsilon-amino group of a conserved lysine residue in the active site. This covalent intermediate, often called the internal aldimine, activates the coenzyme for transamination, decarboxylation, or other reactions. The binding and reactions of the vitamin B6 coenzyme in the catalytic center of aspartate transaminase have been studied as a paradigm for this mechanism. The reversibility of Schiff base formation allows the enzyme to cycle between catalytic states.
Regulation of vitamin B6 and amino acid homeostasis
In simple terms: Some proteins use vitamin B6 binding to keep the cell's vitamin B6 and amino acid levels balanced.
YggS/PLPBP is a conserved PLP-binding protein that plays a role in vitamin B6 and amino acid homeostasis. Its binding of PLP is thought to contribute to sensing or buffering vitamin B6 availability, thereby influencing amino acid metabolism. This homeostatic function distinguishes regulatory PLP-binding proteins from classical PLP-dependent enzymes that use the cofactor for catalysis. Disruption of such regulation can alter cellular responses to vitamin B6 availability.
Downstream effects on gene expression and cell function
In simple terms: Vitamin B6 binding can change how genes are expressed and how cells behave.
Vitamin B6 modulates expression of the albumin gene by inactivating a tissue-specific DNA-binding protein in rat liver, showing that vitamin B6 binding can indirectly affect transcription. In CD8+ T cells, vitamin B6 preserves stemness-like phenotypes and antitumor ability, indicating that vitamin B6 binding and metabolism support immune cell function. In acute myeloid leukemia, vitamin B6 addiction suggests that leukemic cells depend on vitamin B6 binding pathways for survival or proliferation. These downstream effects connect molecular binding events to cell fate and disease.
Pharmacological and antimicrobial modulation
In simple terms: Drugs and antibiotics can interfere with or exploit vitamin B6 binding.
Drug-vitamin B6 interactions can alter vitamin B6 status and drug effects, as reviewed in the context of clinical pharmacology. Vitamin B6 can resensitize mcr-carrying Gram-negative bacteria to colistin, linking vitamin B6 availability and binding to antimicrobial efficacy. Metal complexes containing vitamin B6-based scaffolds can bind DNA and BSA and induce apoptosis in hepatocarcinoma (HepG2) cells, illustrating that vitamin B6-related chemistry can be harnessed for therapeutic purposes. These examples show that vitamin B6 binding is a druggable and modifiable process.
Key Genes Involved in GO:0070279 vitamin B6 binding
The following genes and proteins are representative of vitamin B6 binding (GO:0070279) and its associated biology, based on the verified literature.
| Gene | Major Role | Research Relevance |
|---|---|---|
| YggS/PLPBP | Conserved PLP-binding protein involved in vitamin B6 and amino acid homeostasis | Model for regulatory PLP binding and homeostatic control |
| Aspartate transaminase (GOT1/GOT2) | PLP-dependent enzyme whose catalytic center binds and reacts with the vitamin B6 coenzyme | Classic paradigm for PLP binding and Schiff base chemistry |
| CD8+ T cell vitamin B6 pathway genes | Vitamin B6 preserves stemness-like phenotypes and antitumor ability of CD8+ T cells | Immunometabolism and T cell therapy research |
| Acute myeloid leukemia vitamin B6 addiction genes | Vitamin B6 addiction in acute myeloid leukemia | Cancer metabolism and therapeutic targeting |
| Albumin gene regulatory pathway | Vitamin B6 modulates albumin gene expression by inactivating a tissue-specific DNA-binding protein | Gene regulation and liver biology |
| mcr-carrying Gram-negative bacteria vitamin B6 pathway | Vitamin B6 resensitizes mcr-carrying Gram-negative bacteria to colistin | Antimicrobial resistance and combination therapy |
| Vitamin B6-based metal complex targets | Metal complexes containing vitamin B6-based scaffold bind DNA/BSA and induce apoptosis in HepG2 cells | Hepatocarcinoma and metallodrug research |
| Drug-vitamin B6 interaction targets | Drug-vitamin B6 interaction | Pharmacology and nutrient-drug interaction studies |
| PLP-dependent enzyme family | Binding and reactions of the vitamin B6 coenzyme in catalytic centers | Enzymology and structural biology |
| YggS/PLPBP homologs | Conserved PLP-binding function across species | Comparative genomics and microbial physiology |
| Vitamin B6 homeostasis regulators | Maintain vitamin B6 and amino acid balance | Metabolic regulation and stress response |
| T cell antitumor effectors | Vitamin B6 supports stemness-like phenotypes and antitumor ability | Cancer immunotherapy |
| Leukemia survival pathways | Vitamin B6 addiction supports leukemic cells | Hematologic malignancy research |
| Liver transcription factors | Vitamin B6 inactivates tissue-specific DNA-binding protein | Transcriptional regulation |
| Bacterial colistin resistance modulators | Vitamin B6 resensitizes mcr-carrying bacteria to colistin | Infectious disease and antibiotic adjuvants |
| Hepatocarcinoma apoptosis pathways | Vitamin B6-based complexes induce apoptosis in HepG2 cells | Liver cancer therapy |
| Pharmacological vitamin B6 interactors | Drug-vitamin B6 interaction | Clinical pharmacology and nutrition |
| PLP-binding regulatory proteins | Regulate vitamin B6 and amino acid homeostasis | Systems biology and metabolic modeling |
How Is vitamin B6 binding Regulated?
Vitamin B6 binding and the availability of vitamin B6 compounds are regulated at multiple levels. The conserved PLP-binding protein YggS/PLPBP contributes to vitamin B6 and amino acid homeostasis, indicating that binding proteins can buffer or sense vitamin B6 levels. Drug-vitamin B6 interactions can alter vitamin B6 status and thereby affect binding-dependent processes. In immune cells, vitamin B6 availability influences CD8+ T cell stemness and antitumor ability, suggesting that metabolic and nutritional signals regulate vitamin B6-dependent functions. In acute myeloid leukemia, vitamin B6 addiction implies that leukemic cells have rewired dependencies on vitamin B6 binding and metabolism. Vitamin B6 can also modulate gene expression by inactivating a tissue-specific DNA-binding protein, providing a mechanism by which vitamin B6 status feeds back into transcriptional regulation.
vitamin B6 binding and Human Disease
| Gene | Disease / Biology | Potential Experimental Model |
|---|---|---|
| Vitamin B6 addiction genes | Acute myeloid leukemia | Leukemia cell lines with CRISPR knockout of vitamin B6 binding genes |
| CD8+ T cell vitamin B6 pathway genes | Antitumor immunity and T cell stemness | Primary CD8+ T cells with CRISPR knockout or overexpression |
| mcr-carrying Gram-negative bacteria vitamin B6 pathway | Colistin resistance | Bacterial strains with CRISPR interference or knockout of vitamin B6-related genes |
| Vitamin B6-based metal complex targets | Hepatocarcinoma (HepG2) | HepG2 cells treated with vitamin B6-based metal complexes |
| Albumin gene regulatory pathway | Liver gene regulation | Rat liver models or hepatocyte cell lines with vitamin B6 modulation |
Vitamin B6 binding in cancer and leukemia
Acute myeloid leukemia can exhibit vitamin B6 addiction, meaning leukemic cells depend on vitamin B6 binding and metabolism for survival or proliferation. This dependency suggests that targeting vitamin B6 binding proteins or pathways could be therapeutically useful. In hepatocellular carcinoma, metal complexes containing vitamin B6-based scaffolds can bind DNA and BSA and induce apoptosis in HepG2 cells, indicating that vitamin B6-related chemistry can be directed against liver cancer cells. These findings link GO:0070279 to cancer metabolism and experimental therapeutics.
Vitamin B6 binding in immune function and immunotherapy
Vitamin B6 preserves stemness-like phenotypes and antitumor ability of CD8+ T cells, showing that vitamin B6 binding and metabolism are required for effective T cell responses. This connection places vitamin B6 binding within immunometabolism and cancer immunotherapy research. Understanding how vitamin B6 binding proteins support T cell function may inform strategies to enhance adoptive T cell therapies.
Vitamin B6 binding in infectious disease and antimicrobial resistance
Vitamin B6 can resensitize mcr-carrying Gram-negative bacteria to colistin, linking vitamin B6 availability and binding to antimicrobial efficacy. This observation suggests that vitamin B6-related pathways could be exploited as adjuvants to overcome colistin resistance. Drug-vitamin B6 interactions also highlight the clinical importance of vitamin B6 status during anti-infective or other drug therapy.
Vitamin B6 binding in gene regulation and liver biology
Vitamin B6 modulates expression of the albumin gene by inactivating a tissue-specific DNA-binding protein in rat liver, demonstrating that vitamin B6 binding can indirectly regulate transcription. This mechanism connects vitamin B6 status to liver gene expression and metabolic function. It also illustrates how vitamin B6 binding proteins can influence gene regulatory networks beyond classical cofactor roles.
From vitamin B6 binding-Related Genes to Experimental Models
| Research Question | Suitable Model |
|---|---|
| Does loss of a PLP-binding protein alter vitamin B6 homeostasis? | CRISPR knockout of YggS/PLPBP homologs in cell lines or bacteria |
| Does a specific residue mediate PLP binding and catalysis? | Point mutation of the conserved lysine in PLP-dependent enzymes |
| Can a vitamin B6 binding protein be tagged for localization studies? | Knock-in of an epitope or fluorescent tag at the endogenous locus |
| Does overexpression of a vitamin B6 binding protein change T cell function? | Overexpression of candidate genes in CD8+ T cells |
| Does vitamin B6 addiction create a therapeutic vulnerability? | CRISPR knockout screens in acute myeloid leukemia cells |
| Does vitamin B6 modulate gene expression through DNA-binding proteins? | Knockout or knockdown of the tissue-specific DNA-binding protein in liver cells |
How to Study the vitamin B6 binding Process
| Method | What It Measures | Typical Application |
|---|---|---|
| Isothermal titration calorimetry | Binding affinity and thermodynamics of vitamin B6 compounds to proteins | Confirming direct PLP binding |
| X-ray crystallography | Three-dimensional structure of the binding pocket and Schiff base | Structural characterization of PLP-dependent enzymes |
| CRISPR knockout | Loss-of-function phenotype of vitamin B6 binding genes | Testing homeostatic and addiction roles |
| CRISPR point mutation | Effect of specific residues on binding and catalysis | Dissecting catalytic lysine function |
| Metabolomics | Levels of vitamin B6 compounds and amino acids | Assessing homeostasis upon perturbation |
| RNA-seq | Transcriptional changes downstream of vitamin B6 binding | Identifying gene expression effects |
| Flow cytometry | CD8+ T cell stemness and antitumor phenotypes | Immunometabolism studies |
| Antimicrobial susceptibility testing | Colistin resensitization by vitamin B6 | Antibiotic adjuvant discovery |
Biochemical and structural methods for vitamin B6 binding
Biochemical assays such as equilibrium dialysis, isothermal titration calorimetry, and spectrophotometric titration can measure binding of PLP and other vitamin B6 compounds to purified proteins. Structural methods including X-ray crystallography and NMR can reveal the binding pocket and Schiff base geometry, as established for aspartate transaminase. These approaches are essential for confirming that a protein directly binds vitamin B6 compounds and for defining the molecular determinants of GO:0070279.
Genetic and CRISPR-based functional methods
CRISPR knockout, point mutation, knock-in, and overexpression can be used to test the function of candidate vitamin B6 binding proteins in cells. For example, knockout of YggS/PLPBP homologs can reveal effects on vitamin B6 and amino acid homeostasis, while CRISPR screens in acute myeloid leukemia cells can identify vitamin B6 addiction dependencies. These genetic approaches complement biochemical binding assays by linking binding to phenotype.
Metabolic and transcriptomic profiling
Metabolomics can quantify vitamin B6 compounds and amino acids to assess homeostatic changes upon perturbation of vitamin B6 binding proteins. RNA-seq can reveal downstream transcriptional effects, such as modulation of albumin gene expression by vitamin B6. Combining metabolomics and transcriptomics provides a systems-level view of how vitamin B6 binding influences cellular states.
Immunological and antimicrobial assays
Flow cytometry and functional assays can measure CD8+ T cell stemness and antitumor ability under conditions of vitamin B6 modulation. Antimicrobial susceptibility testing can determine whether vitamin B6 resensitizes mcr-carrying Gram-negative bacteria to colistin. These assays connect vitamin B6 binding to immune function and infectious disease outcomes.
How CRISPR Can Be Used to Study GO:0070279 vitamin B6 binding
Knockout
CRISPR knockout of genes encoding vitamin B6 binding proteins, such as YggS/PLPBP homologs, can reveal their roles in vitamin B6 and amino acid homeostasis. Knockout screens in acute myeloid leukemia cells can identify vitamin B6 addiction dependencies. These models are useful for testing whether a candidate gene is required for vitamin B6 binding-related phenotypes.
Point Mutation
CRISPR point mutation can be used to alter specific residues involved in vitamin B6 binding, such as the conserved lysine that forms a Schiff base with PLP in aspartate transaminase. Such mutations allow researchers to separate binding from catalysis and to test the functional consequences of impaired vitamin B6 binding. Point mutation models are also valuable for studying regulatory PLP-binding proteins.
Knock-in
CRISPR knock-in can be used to tag endogenous vitamin B6 binding proteins with epitopes or fluorescent reporters for localization and interaction studies. Knock-in of disease-relevant mutations can model human variants that affect vitamin B6 binding. These models help connect molecular binding events to cellular and organismal phenotypes.
Overexpression
CRISPR overexpression or cDNA overexpression of vitamin B6 binding proteins can test gain-of-function effects, such as enhanced CD8+ T cell stemness and antitumor ability. Overexpression can also be used to study vitamin B6-dependent gene regulation, such as modulation of albumin gene expression. These approaches complement loss-of-function studies to establish causality.
How EDITGENE Supports vitamin B6 binding Research
Researchers studying vitamin B6 binding-related genes often need to determine whether a candidate gene is causally involved in vitamin B6-dependent phenotypes, such as metabolic homeostasis, immune cell function, or cancer cell survival. Establishing causality requires precise genetic models that can knockout, mutate, tag, or overexpress the gene of interest in relevant cell types. EDITGENE provides a comprehensive suite of CRISPR services to support such studies, from single-gene editing to genome-wide library screening and bioinformatics analysis.
Contact EDITGENE today to design your custom CRISPR model for vitamin B6 binding research.
Frequently Asked Questions About vitamin B6 binding
What is GO:0070279 vitamin B6 binding?
GO:0070279 is a Gene Ontology molecular_function term defined as binding to a vitamin B6 compound: pyridoxal, pyridoxamine, pyridoxine, or the active form, pyridoxal phosphate.
What genes are involved in vitamin B6 binding?
Genes encoding PLP-dependent enzymes such as aspartate transaminase, the conserved PLP-binding protein YggS/PLPBP, and other vitamin B6 binding proteins are involved.
What is the active form of vitamin B6 that binds proteins?
Pyridoxal phosphate (PLP) is the active coenzyme form of vitamin B6 that binds to proteins.
How does vitamin B6 binding affect immune cells?
Vitamin B6 preserves stemness-like phenotypes and antitumor ability of CD8+ T cells, indicating that vitamin B6 binding and metabolism support T cell function.
Is vitamin B6 binding important in cancer?
Yes, acute myeloid leukemia can exhibit vitamin B6 addiction, and vitamin B6-based metal complexes can induce apoptosis in hepatocarcinoma cells.
Can vitamin B6 binding be studied with CRISPR?
Yes, CRISPR knockout, point mutation, knock-in, and overexpression can be used to study genes encoding vitamin B6 binding proteins.
What is the role of YggS/PLPBP in vitamin B6 binding?
YggS/PLPBP is a conserved PLP-binding protein that plays a role in vitamin B6 and amino acid homeostasis.
How does vitamin B6 modulate gene expression?
Vitamin B6 modulates expression of the albumin gene by inactivating a tissue-specific DNA-binding protein in rat liver.
Do drugs interact with vitamin B6 binding?
Drug-vitamin B6 interactions are documented and can affect vitamin B6 status and drug effects.
Can vitamin B6 affect antibiotic resistance?
Vitamin B6 can resensitize mcr-carrying Gram-negative bacteria to colistin, linking vitamin B6 to antimicrobial efficacy.
Conclusion
GO:0070279 (vitamin B6 binding) is a molecular_function term that captures the physical interaction between proteins and vitamin B6 compounds, including the active coenzyme PLP. This binding underlies diverse biological processes, from classical PLP-dependent catalysis in aspartate transaminase to homeostatic regulation by YggS/PLPBP, immune support in CD8+ T cells, and vitamin B6 addiction in acute myeloid leukemia. Vitamin B6 binding also intersects with gene regulation, drug interactions, antimicrobial resistance, and metal-based anticancer agents. Researchers can leverage CRISPR knockout, point mutation, knock-in, overexpression, and library screening to dissect the causal roles of vitamin B6 binding proteins in health and disease.
References
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- 3. Ito T. 2022. Role of the conserved pyridoxal 5'-phosphate-binding protein YggS/PLPBP in vitamin B6 and amino acid homeostasis.. Biosci Biotechnol Biochem 86(9):1183-1191 PMID: 35803498
- 4. Xu T et al.. 2025. Vitamin B6 resensitizes mcr-carrying Gram-negative bacteria to colistin.. Commun Biol 8(1):459 PMID: 40108411
- 5. BRAUNSTEIN AE. 1964. BINDING AND REACTIONS OF THE VITAMIN B6 COENZYME IN THE CATALYTIC CENTER OF ASPARTATE TRANSAMINASE.. Vitam Horm 22:451-84 PMID: 14284115
- 6. Alroba AAN et al.. 2025. Metal complexes containing vitamin B6-based scaffold as potential DNA/BSA-binding agents inducing apoptosis in hepatocarcinoma (HepG2) cells.. Mol Divers 29(5):4019-4042 PMID: 39289257
- 7. Chen CC et al.. 2020. Vitamin B6 Addiction in Acute Myeloid Leukemia.. Cancer Cell 37(1):71-84.e7 PMID: 31935373
- 8. Oka T et al.. 1995. Vitamin B6 modulates expression of albumin gene by inactivating tissue-specific DNA-binding protein in rat liver.. Biochem J 309 ( Pt 1)(Pt 1):243-8 PMID: 7619063
