The research report should be a detailed narrative explaining the function, biological processes, and localization of the gene product. Citations should be given for all claims.
You should prioritize authoritative reviews and primary scientific literature when conducting research. You can supplement
this with annotations you find in gene/protein databases, but these can be outdated or inaccurate.
We are specifically interested in the primary function of the gene - for enzymes, what reaction is catalyzed, and what is the substrate specificity? For transporters, what is the substrate? For structural proteins or adapters, what is the broader structural role? For signaling molecules, what is the role in the pathway.
We are interested in where in or outside the cell the gene product carries out its function.
We are also interested in the signaling or biochemical pathways in which the gene functions. We are less interested in broad pleiotropic effects, except where these elucidate the precise role.
Include evidence where possible. We are interested in both experimental evidence as well as inference from structure, evolution, or bioinformatic analysis. Precise studies should be prioritized over high-throughput, where available.
BCAT3 (UniProt: Q9M401, Locus: At3g49680) encodes a plastid-localized branched-chain amino acid aminotransferase in Arabidopsis thaliana (knill2008arabidopsisbranchedchainaminotransferase pages 1-2, diebold2002thebranchedchainamino pages 5-8). This enzyme belongs to the class-IV pyridoxal-phosphate-dependent aminotransferase family and is part of a small gene family of six to seven BCAT genes in Arabidopsis (diebold2002thebranchedchainamino pages 3-5, knill2008arabidopsisbranchedchainaminotransferase pages 1-2).
BCAT3 is a pyridoxal-5'-phosphate (PLP)-dependent enzyme that catalyzes reversible transamination reactions, converting 2-oxo acids to their corresponding amino acids (knill2008arabidopsisbranchedchainaminotransferase pages 1-2). The enzyme operates through the characteristic ping-pong bi-bi mechanism of PLP-dependent aminotransferases, in which the amino acid substrate reacts with enzyme-bound PLP to generate pyridoxamine phosphate (PMP) and release a keto acid product; subsequently, a keto acid substrate reacts with PMP to regenerate PLP and produce the corresponding amino acid (koper2022evolutionaryoriginand pages 7-8).
BCAT3 exhibits highest catalytic activity toward the branched-chain amino acid (BCAA) precursors. Detailed kinetic characterization of recombinant BCAT3 revealed the following substrate preferences (knill2008arabidopsisbranchedchainaminotransferase pages 2-3):
These kinetic parameters demonstrate that BCAT3 catalyzes the terminal transamination step in BCAA biosynthesis, producing leucine, isoleucine, and valine from their respective 2-oxo acid precursors (knill2008arabidopsisbranchedchainaminotransferase pages 3-4, knill2008arabidopsisbranchedchainaminotransferase pages 1-2).
Importantly, BCAT3 also demonstrates substantial activity toward intermediates of the methionine chain elongation pathway (knill2008arabidopsisbranchedchainaminotransferase pages 3-4, knill2008arabidopsisbranchedchainaminotransferase pages 8-10). The enzyme converts:
This dual substrate specificity enables BCAT3 to function at the intersection of primary amino acid metabolism and secondary glucosinolate biosynthesis (knill2008arabidopsisbranchedchainaminotransferase pages 1-2).
| Substrate name | Abbreviation | Reported Km (mM) | Reported Vmax or relative activity | Biological pathway / inferred BCAT3 role |
|---|---|---|---|---|
| 4-Methyl-2-oxopentanoate (α-ketoisocaproate; leucine-related 2-oxo acid) | 4MOP / KIC | 0.14 | Vmax: 27.42 mmol·min⁻¹·mg⁻¹ as reported; relative activity: 1,565% at 0.1 mM and 353% at 2 mM | Preferred canonical substrate; terminal transamination produces leucine in plastidial branched-chain amino-acid biosynthesis. (knill2008arabidopsisbranchedchainaminotransferase pages 3-4, knill2008arabidopsisbranchedchainaminotransferase pages 2-3) |
| 3-Methyl-2-oxopentanoate (α-keto-β-methylvalerate; isoleucine-related 2-oxo acid) | 3MOP / KMV | 0.14 | Vmax: 13.33 mmol·min⁻¹·mg⁻¹ as reported; relative activity: 875% at 0.1 mM and 328% at 2 mM | High-affinity canonical substrate; terminal transamination produces isoleucine in plastidial branched-chain amino-acid biosynthesis. (knill2008arabidopsisbranchedchainaminotransferase pages 3-4, knill2008arabidopsisbranchedchainaminotransferase pages 2-3) |
| 3-Methyl-2-oxobutanoate (α-ketoisovalerate; valine-related 2-oxo acid) | 3MOB / KIV | 1.38 | Relative activity: 182% at 0.1 mM and 136% at 2 mM | Terminal transamination produces valine; reduced free valine in the bcat3-1 mutant supports an in-planta role despite lower affinity than for 4MOP and 3MOP. (knill2008arabidopsisbranchedchainaminotransferase pages 3-4, knill2008arabidopsisbranchedchainaminotransferase pages 2-3, knill2008arabidopsisbranchedchainaminotransferase pages 7-8) |
| 4-Methylthio-2-oxobutanoate (methionine 2-oxo acid) | MTOB | 1.92 | Relative activity: 100% at both 0.1 and 2 mM—the normalization reference in the reported assay | Methionine-chain-elongation entry intermediate; BCAT3 can catalyze its reversible interconversion with methionine and may partially compensate for cytosolic BCAT4 when BCAT4 is absent. (knill2008arabidopsisbranchedchainaminotransferase pages 3-4, knill2008arabidopsisbranchedchainaminotransferase pages 2-3, knill2008arabidopsisbranchedchainaminotransferase pages 1-2) |
| 5-Methylthio-2-oxopentanoate | MTOP | Not reported in the cited study | Relative activity: 109% at 0.1 mM and 112% at 2 mM | Transamination produces homomethionine, helping terminate a short methionine-chain-elongation cycle and supplying precursors for short-chain aliphatic glucosinolates. (knill2008arabidopsisbranchedchainaminotransferase pages 3-4, knill2008arabidopsisbranchedchainaminotransferase pages 8-10) |
| 6-Methylthio-2-oxohexanoate | MTOH | Not reported in the cited study | Relative activity: 62% at 0.1 mM and 86% at 2 mM | Transamination produces dihomomethionine; contributes to methionine-derived aliphatic glucosinolate biosynthesis and influences glucosinolate side-chain-length distribution. (knill2008arabidopsisbranchedchainaminotransferase pages 3-4, knill2008arabidopsisbranchedchainaminotransferase pages 8-10) |
Table: Kinetic and relative-activity data show that Arabidopsis BCAT3 favors canonical branched-chain 2-oxo acids but also accepts methionine-chain-elongation intermediates. This substrate breadth supports its dual role in branched-chain amino-acid and aliphatic glucosinolate biosynthesis.
BCAT3 is targeted to and functions within plastids (chloroplasts) (diebold2002thebranchedchainamino pages 5-8, knill2008arabidopsisbranchedchainaminotransferase pages 1-2, diebold2002thebranchedchainamino pages 1-2). This localization was established through multiple experimental approaches:
GFP fusion studies: Transient expression of BCAT3-GFP fusion proteins in tobacco protoplasts demonstrated colocalization with chloroplast autofluorescence (diebold2002thebranchedchainamino pages 5-8)
Targeting sequence prediction: The N-terminal sequence contains a plastid transit peptide consistent with chloroplast import (schuster2006branchedchainaminotransferase4is pages 1-2, diebold2002thebranchedchainamino pages 3-5)
Functional colocalization: BCAT3 colocalizes with other plastid enzymes including RidA (reactive intermediate deaminase) and threonine dehydratase, supporting its role in plastid-localized BCAA biosynthesis (niehaus2014arabidopsisandmaize pages 5-6, niehaus2014arabidopsisandmaize pages 1-2, niehaus2014arabidopsisandmaize pages 11-12)
The plastid localization is functionally significant because this is the cellular compartment where both BCAA biosynthesis and the methionine chain elongation pathway predominantly occur (knill2008arabidopsisbranchedchainaminotransferase pages 1-2, knill2008arabidopsisbranchedchainaminotransferase pages 8-10).
BCAT3 has the unique characteristic of participating in both primary amino acid metabolism and secondary metabolite biosynthesis, demonstrating the interconnection between these traditionally separate metabolic categories (knill2008arabidopsisbranchedchainaminotransferase pages 1-2, knill2008arabidopsisbranchedchainaminotransferase pages 2-3, knill2008arabidopsisbranchedchainaminotransferase pages 8-10).
In primary metabolism, BCAT3 catalyzes the terminal transamination reactions producing leucine, isoleucine, and valine (knill2008arabidopsisbranchedchainaminotransferase pages 1-2). Evidence from bcat3-1 knockout mutants revealed:
The enzyme's lower affinity for the valine precursor 3MOB (Km = 1.38 mM) compared to the leucine biosynthesis enzyme isopropylmalate synthase (Km ≈ 0.3 mM) may represent substrate competition that helps preserve 3MOB for leucine biosynthesis (knill2008arabidopsisbranchedchainaminotransferase pages 7-8).
BCAT3 plays a critical role in determining glucosinolate chain length by catalyzing terminal transamination steps in the methionine chain elongation cycle (knill2008arabidopsisbranchedchainaminotransferase pages 8-10, knill2008arabidopsisbranchedchainaminotransferase pages 7-8). The enzyme preferentially transaminates shorter-chain keto acids, particularly MTOP and MTOH, converting them to homomethionine and dihomomethionine, respectively (knill2008arabidopsisbranchedchainaminotransferase pages 8-10).
Metabolite profiling of bcat3-1 mutants demonstrated:
These changes indicate that in wild-type plants, BCAT3 preferentially terminates the chain elongation cycle at shorter lengths by transaminating the corresponding keto acids. In the absence of BCAT3, keto acids persist and undergo additional elongation cycles, producing longer-chain glucosinolates (knill2008arabidopsisbranchedchainaminotransferase pages 7-8).
BCAT3 demonstrates partial functional overlap with BCAT4, the cytosolic enzyme that catalyzes the initial transamination of methionine to MTOB (knill2008arabidopsisbranchedchainaminotransferase pages 1-2). Analysis of bcat3-1/bcat4-2 double mutants revealed:
BCAT3 works in concert with methylthioalkylmalate synthases (MAM1 and MAM3), which catalyze the condensation reactions that extend the methionine carbon chain before BCAT3 performs the terminal transamination (knill2008arabidopsisbranchedchainaminotransferase pages 8-10, knill2008arabidopsisbranchedchainaminotransferase pages 7-8).
Arabidopsis contains six to seven BCAT genes (BCAT1-BCAT7), which share 47.5-84.1% amino acid identity with one another (diebold2002thebranchedchainamino pages 3-5, diebold2002thebranchedchainamino pages 2-3, diebold2002thebranchedchainamino pages 1-2). BCAT3 is particularly similar to BCAT4 (80.9% identity), suggesting recent gene duplication and subsequent functional specialization (diebold2002thebranchedchainamino pages 3-5).
The family has diversified through subcellular compartmentation rather than substrate specialization alone (diebold2002thebranchedchainamino pages 5-8, schuster2006branchedchainaminotransferase4is pages 1-2):
| Gene name | Locus ID | Subcellular localization | Primary function/pathway | Key distinguishing features |
|---|---|---|---|---|
| BCAT1 | At1g10070 | Mitochondrion | Branched-chain amino-acid (BCAA) catabolism | Mitochondrial isoform associated with initiation of Leu, Ile, and Val degradation; contrasts with the predominantly biosynthetic plastidial isoforms. (diebold2002thebranchedchainamino pages 5-8, knill2008arabidopsisbranchedchainaminotransferase pages 1-2) |
| BCAT2 | At1g10060 | Plastid/chloroplast | BCAA biosynthesis | One of three experimentally assigned plastidial BCATs; functional complementation supports BCAA aminotransferase activity, but its individual in-planta substrate preference remains incompletely resolved. (diebold2002thebranchedchainamino pages 2-3, diebold2002thebranchedchainamino pages 1-2) |
| BCAT3 | At3g49680 | Plastid/chloroplast | BCAA biosynthesis and methionine-derived aliphatic glucosinolate biosynthesis | Target protein corresponding to UniProt Q9M401; active with all three canonical branched-chain 2-oxo acids and with methionine-chain-elongation intermediates. It preferentially terminates shorter chain-elongation cycles and can partially compensate for BCAT4 loss. (knill2008arabidopsisbranchedchainaminotransferase pages 1-2) |
| BCAT4 | At3g19710 | Cytosol | Initiation of methionine chain elongation for aliphatic glucosinolate biosynthesis | Specialized toward Met and related substrates; catalyzes the initial conversion of Met to 4-methylthio-2-oxobutanoate. It is closely related to BCAT3 but differs in compartmentation and preferred pathway role. (schuster2006branchedchainaminotransferase4is pages 1-2, schuster2006branchedchainaminotransferase4is pages 2-3) |
| BCAT5 | At5g65780 | Plastid/chloroplast | Probable BCAA biosynthesis | Plastidial and capable of complementing BCAT-deficient yeast; its precise physiological substrate specialization relative to BCAT2 and BCAT3 remains unresolved. (diebold2002thebranchedchainamino pages 5-8, diebold2002thebranchedchainamino pages 1-2) |
| BCAT6 | At1g50110 | Cytosol, proposed | Cytosolic amino-acid and methionine-related metabolism | Lacks a clear organellar targeting peptide and complements BCAT-deficient yeast. Its detailed physiological role was less firmly established in the foundational family studies. (diebold2002thebranchedchainamino pages 2-3, schuster2006branchedchainaminotransferase4is pages 1-2, maloney2010characterizationofthe pages 1-2) |
| BCAT7 | At1g50090 | Unresolved | Unresolved; putative BCAT-family member | Predicted seventh family member and highly similar to BCAT6, but no cDNA was recovered in the original characterization; consequently, transcription, localization, and enzymatic function were not established. Later literature commonly describes six transcribed BCAT genes rather than seven confirmed functional members. (diebold2002thebranchedchainamino pages 3-5, diebold2002thebranchedchainamino pages 2-3, knill2008arabidopsisbranchedchainaminotransferase pages 1-2) |
Table: Comparison of the seven proposed Arabidopsis BCAT-family loci, emphasizing their compartmental and functional specialization. BCAT3 is distinguished by its experimentally supported dual role in plastidial BCAA and glucosinolate-precursor metabolism.
BCATs belong to aminotransferase class III and PLP fold type IV, evolutionarily distinct from most other aminotransferases (koper2022evolutionaryoriginand pages 7-8, koper2022evolutionaryoriginand pages 8-11, koper2022evolutionaryoriginand pages 6-7). The structural architecture includes a smaller N-terminal domain with a six-stranded antiparallel β-sheet and a larger C-terminal domain containing a pseudo-β-barrel and the active-site lysine for PLP binding (koper2022evolutionaryoriginand pages 7-8, koper2022evolutionaryoriginand pages 8-11). BCATs typically function as homodimers and can further oligomerize into hexamers (koper2022evolutionaryoriginand pages 7-8).
The evolutionary connection between leucine biosynthesis and methionine chain elongation is reflected in the recruitment of related enzyme families (BCATs and MAMs) for both pathways, suggesting a common evolutionary origin (schuster2006branchedchainaminotransferase4is pages 1-2, schuster2006branchedchainaminotransferase4is pages 2-3).
BCAT3 is absolutely dependent on pyridoxal-5'-phosphate (PLP) as a cofactor (knill2008arabidopsisbranchedchainaminotransferase pages 1-2, binder2010branchedchainaminoacid pages 7-8). The enzyme belongs to PLP fold type IV, where PLP binds in the opposite orientation compared to type I aminotransferases, resulting in distinctive substrate stereospecificity (koper2022evolutionaryoriginand pages 7-8). The active-site lysine forms a Schiff-base linkage (internal aldimine) with PLP, and a conserved glutamic acid interacts with the PLP ring nitrogen (koper2022evolutionaryoriginand pages 7-8).
The catalytic mechanism proceeds through:
1. Formation of external aldimine with the amino acid substrate
2. Direct conversion to ketimine through 1,3-prototropic shift (characteristic of class III enzymes)
3. Hydrolysis to release the keto acid product and generate PMP
4. Reverse reaction with a keto acid substrate to regenerate PLP and the amino acid product (koper2022evolutionaryoriginand pages 7-8, koper2022evolutionaryoriginand pages 8-11)
BCAT3 is vulnerable to inactivation by reactive enamine/imine intermediates generated when threonine dehydratase acts on serine, producing 2-iminopropanoate (niehaus2014arabidopsisandmaize pages 5-6, niehaus2014arabidopsisandmaize pages 3-5, niehaus2014arabidopsisandmaize pages 1-2). This reactive intermediate can attack the PLP cofactor of BCAT3, forming an adduct that inactivates the enzyme (niehaus2014arabidopsisandmaize pages 2-3).
The plastid-localized RidA (Reactive Intermediate Deaminase A) protein protects BCAT3 by hydrolyzing these reactive enamine/imine intermediates before they can damage the aminotransferase (niehaus2014arabidopsisandmaize pages 5-6, niehaus2014arabidopsisandmaize pages 3-5, niehaus2014arabidopsisandmaize pages 6-8). In vitro experiments demonstrated:
RidA knockout plants show reduced root growth, accumulation of 2-oxobutanoate, and isoleucine deficiency, consistent with impaired BCAT3 function in BCAA biosynthesis (niehaus2014arabidopsisandmaize pages 6-8, niehaus2014arabidopsisandmaize pages 8-9). The strong correlation between RidA and BCAT3 gene expression supports their functional coupling in plastids (niehaus2014arabidopsisandmaize pages 2-3, niehaus2014arabidopsisandmaize pages 11-12).
Limited information is available about BCAT3 expression patterns, but key observations include:
These expression patterns are consistent with roles in both vascular transport of amino acids and glucosinolate defense metabolism.
The functional characterization of BCAT3 rests on multiple complementary experimental approaches:
While the foundational work on BCAT3 was conducted primarily between 2002-2008, recent reviews have provided important evolutionary and mechanistic context:
Koper et al. (2022) placed plant BCATs within the broader evolutionary framework of aminotransferases, emphasizing their broad substrate specificity and the retention of catalytic promiscuity that enables enzymes like BCAT3 to function across multiple metabolic pathways (koper2022evolutionaryoriginand pages 1-2). This review highlighted that some isoforms of plant BCATs, including BCAT3 and BCAT6, have substantial activity toward non-canonical substrates, supporting the concept of metabolic pathway interconnection.
Niehaus et al. (2014) established the importance of RidA-mediated protection for plastidial BCAA biosynthesis, revealing that BCAT3 requires protective mechanisms to function effectively in the presence of threonine dehydratase (niehaus2014arabidopsisandmaize pages 5-6, niehaus2014arabidopsisandmaize pages 3-5, niehaus2014arabidopsisandmaize pages 1-2). This work demonstrated that metabolic enzyme function depends not only on intrinsic catalytic properties but also on cellular systems that prevent collateral damage from reactive metabolic intermediates.
BCAT3 (At3g49680) in Arabidopsis thaliana is a plastid-localized, PLP-dependent branched-chain aminotransferase with the following key functional characteristics:
Primary Function: BCAT3 catalyzes reversible transamination reactions converting branched-chain 2-oxo acids to their corresponding amino acids (leucine, isoleucine, valine) and methionine chain elongation intermediates to chain-extended methionine derivatives (homomethionine, dihomomethionine).
Substrate Specificity: The enzyme shows highest affinity for 4-methyl-2-oxopentanoate (leucine precursor; Km = 0.14 mM) and 3-methyl-2-oxopentanoate (isoleucine precursor; Km = 0.14 mM), with lower but significant activity toward valine precursor (Km = 1.38 mM) and methionine chain elongation intermediates.
Subcellular Localization: BCAT3 functions exclusively in plastids (chloroplasts), where it has access to both BCAA biosynthetic substrates and methionine chain elongation intermediates.
Biochemical Pathways: The enzyme operates at the intersection of primary and secondary metabolism, participating in both BCAA biosynthesis (terminal transamination step) and methionine-derived aliphatic glucosinolate biosynthesis (terminal transamination in the chain elongation cycle). BCAT3 preferentially terminates shorter chain elongation cycles, thereby influencing glucosinolate chain length distribution.
Evolutionary Context: BCAT3 is part of a six-member gene family (BCAT1-6) in Arabidopsis that has diversified primarily through subcellular compartmentation. It is most closely related to BCAT4 (80.9% identity) but differs in localization (plastid vs. cytosol) and preferred pathway role.
Regulatory Protection: BCAT3 requires protection from reactive enamine/imine intermediates by the RidA enzyme to maintain full catalytic activity in plastids.
This dual functionality demonstrates that single enzymes can serve as critical links between primary amino acid metabolism and specialized secondary metabolism, challenging traditional boundaries between these metabolic categories. The preferential substrate specificity of BCAT3 for shorter-chain intermediates provides a mechanism for regulating glucosinolate structural diversity, with important implications for plant defense chemistry.
References
(knill2008arabidopsisbranchedchainaminotransferase pages 1-2): Tanja Knill, Joachim Schuster, Michael Reichelt, Jonathan Gershenzon, and Stefan Binder. Arabidopsis branched-chain aminotransferase 3 functions in both amino acid and glucosinolate biosynthesis. Plant Physiology, 146:1028-1039, Dec 2007. URL: https://doi.org/10.1104/pp.107.111609, doi:10.1104/pp.107.111609. This article has 143 citations and is from a highest quality peer-reviewed journal.
(diebold2002thebranchedchainamino pages 5-8): Ruth Diebold, Joachim Schuster, Klaus Däschner, and Stefan Binder. The branched-chain amino acid transaminase gene family in arabidopsis encodes plastid and mitochondrial proteins1. Plant Physiology, 129:540-550, Jun 2002. URL: https://doi.org/10.1104/pp.001602, doi:10.1104/pp.001602. This article has 191 citations and is from a highest quality peer-reviewed journal.
(diebold2002thebranchedchainamino pages 3-5): Ruth Diebold, Joachim Schuster, Klaus Däschner, and Stefan Binder. The branched-chain amino acid transaminase gene family in arabidopsis encodes plastid and mitochondrial proteins1. Plant Physiology, 129:540-550, Jun 2002. URL: https://doi.org/10.1104/pp.001602, doi:10.1104/pp.001602. This article has 191 citations and is from a highest quality peer-reviewed journal.
(koper2022evolutionaryoriginand pages 7-8): Kaan Koper, Sang-Woo Han, Delia Casas Pastor, Yasuo Yoshikuni, and Hiroshi A. Maeda. Evolutionary origin and functional diversification of aminotransferases. Journal of Biological Chemistry, 298:102122, Aug 2022. URL: https://doi.org/10.1016/j.jbc.2022.102122, doi:10.1016/j.jbc.2022.102122. This article has 104 citations and is from a domain leading peer-reviewed journal.
(knill2008arabidopsisbranchedchainaminotransferase pages 2-3): Tanja Knill, Joachim Schuster, Michael Reichelt, Jonathan Gershenzon, and Stefan Binder. Arabidopsis branched-chain aminotransferase 3 functions in both amino acid and glucosinolate biosynthesis. Plant Physiology, 146:1028-1039, Dec 2007. URL: https://doi.org/10.1104/pp.107.111609, doi:10.1104/pp.107.111609. This article has 143 citations and is from a highest quality peer-reviewed journal.
(knill2008arabidopsisbranchedchainaminotransferase pages 3-4): Tanja Knill, Joachim Schuster, Michael Reichelt, Jonathan Gershenzon, and Stefan Binder. Arabidopsis branched-chain aminotransferase 3 functions in both amino acid and glucosinolate biosynthesis. Plant Physiology, 146:1028-1039, Dec 2007. URL: https://doi.org/10.1104/pp.107.111609, doi:10.1104/pp.107.111609. This article has 143 citations and is from a highest quality peer-reviewed journal.
(knill2008arabidopsisbranchedchainaminotransferase pages 8-10): Tanja Knill, Joachim Schuster, Michael Reichelt, Jonathan Gershenzon, and Stefan Binder. Arabidopsis branched-chain aminotransferase 3 functions in both amino acid and glucosinolate biosynthesis. Plant Physiology, 146:1028-1039, Dec 2007. URL: https://doi.org/10.1104/pp.107.111609, doi:10.1104/pp.107.111609. This article has 143 citations and is from a highest quality peer-reviewed journal.
(knill2008arabidopsisbranchedchainaminotransferase pages 7-8): Tanja Knill, Joachim Schuster, Michael Reichelt, Jonathan Gershenzon, and Stefan Binder. Arabidopsis branched-chain aminotransferase 3 functions in both amino acid and glucosinolate biosynthesis. Plant Physiology, 146:1028-1039, Dec 2007. URL: https://doi.org/10.1104/pp.107.111609, doi:10.1104/pp.107.111609. This article has 143 citations and is from a highest quality peer-reviewed journal.
(diebold2002thebranchedchainamino pages 1-2): Ruth Diebold, Joachim Schuster, Klaus Däschner, and Stefan Binder. The branched-chain amino acid transaminase gene family in arabidopsis encodes plastid and mitochondrial proteins1. Plant Physiology, 129:540-550, Jun 2002. URL: https://doi.org/10.1104/pp.001602, doi:10.1104/pp.001602. This article has 191 citations and is from a highest quality peer-reviewed journal.
(schuster2006branchedchainaminotransferase4is pages 1-2): Joachim Schuster, Tanja Knill, Michael Reichelt, Jonathan Gershenzon, and Stefan Binder. Branched-chain aminotransferase4 is part of the chain elongation pathway in the biosynthesis of methionine-derived glucosinolates in arabidopsis. The Plant Cell, 18(10):2664-2679, Oct 2006. URL: https://doi.org/10.1105/tpc.105.039339, doi:10.1105/tpc.105.039339. This article has 254 citations.
(niehaus2014arabidopsisandmaize pages 5-6): Thomas D. Niehaus, Thuy N.D. Nguyen, Satinder K. Gidda, Mona ElBadawi-Sidhu, Jennifer A. Lambrecht, Donald R. McCarty, Diana M. Downs, Arthur J.L. Cooper, Oliver Fiehn, Robert T. Mullen, and Andrew D. Hanson. arabidopsis and maize rida proteins preempt reactive enamine/imine damage to branched-chain amino acid biosynthesis in plastids. Jul 2014. URL: https://doi.org/10.1105/tpc.114.126854, doi:10.1105/tpc.114.126854. This article has 75 citations.
(niehaus2014arabidopsisandmaize pages 1-2): Thomas D. Niehaus, Thuy N.D. Nguyen, Satinder K. Gidda, Mona ElBadawi-Sidhu, Jennifer A. Lambrecht, Donald R. McCarty, Diana M. Downs, Arthur J.L. Cooper, Oliver Fiehn, Robert T. Mullen, and Andrew D. Hanson. arabidopsis and maize rida proteins preempt reactive enamine/imine damage to branched-chain amino acid biosynthesis in plastids. Jul 2014. URL: https://doi.org/10.1105/tpc.114.126854, doi:10.1105/tpc.114.126854. This article has 75 citations.
(niehaus2014arabidopsisandmaize pages 11-12): Thomas D. Niehaus, Thuy N.D. Nguyen, Satinder K. Gidda, Mona ElBadawi-Sidhu, Jennifer A. Lambrecht, Donald R. McCarty, Diana M. Downs, Arthur J.L. Cooper, Oliver Fiehn, Robert T. Mullen, and Andrew D. Hanson. arabidopsis and maize rida proteins preempt reactive enamine/imine damage to branched-chain amino acid biosynthesis in plastids. Jul 2014. URL: https://doi.org/10.1105/tpc.114.126854, doi:10.1105/tpc.114.126854. This article has 75 citations.
(diebold2002thebranchedchainamino pages 2-3): Ruth Diebold, Joachim Schuster, Klaus Däschner, and Stefan Binder. The branched-chain amino acid transaminase gene family in arabidopsis encodes plastid and mitochondrial proteins1. Plant Physiology, 129:540-550, Jun 2002. URL: https://doi.org/10.1104/pp.001602, doi:10.1104/pp.001602. This article has 191 citations and is from a highest quality peer-reviewed journal.
(schuster2006branchedchainaminotransferase4is pages 2-3): Joachim Schuster, Tanja Knill, Michael Reichelt, Jonathan Gershenzon, and Stefan Binder. Branched-chain aminotransferase4 is part of the chain elongation pathway in the biosynthesis of methionine-derived glucosinolates in arabidopsis. The Plant Cell, 18(10):2664-2679, Oct 2006. URL: https://doi.org/10.1105/tpc.105.039339, doi:10.1105/tpc.105.039339. This article has 254 citations.
(maloney2010characterizationofthe pages 1-2): Gregory S. Maloney, Andrej Kochevenko, Denise M. Tieman, Takayuki Tohge, Uri Krieger, Dani Zamir, Mark G. Taylor, Alisdair R. Fernie, and Harry J. Klee. Characterization of the branched-chain amino acid aminotransferase enzyme family in tomato. Plant Physiology, 153:925-936, Apr 2010. URL: https://doi.org/10.1104/pp.110.154922, doi:10.1104/pp.110.154922. This article has 141 citations and is from a highest quality peer-reviewed journal.
(koper2022evolutionaryoriginand pages 8-11): Kaan Koper, Sang-Woo Han, Delia Casas Pastor, Yasuo Yoshikuni, and Hiroshi A. Maeda. Evolutionary origin and functional diversification of aminotransferases. Journal of Biological Chemistry, 298:102122, Aug 2022. URL: https://doi.org/10.1016/j.jbc.2022.102122, doi:10.1016/j.jbc.2022.102122. This article has 104 citations and is from a domain leading peer-reviewed journal.
(koper2022evolutionaryoriginand pages 6-7): Kaan Koper, Sang-Woo Han, Delia Casas Pastor, Yasuo Yoshikuni, and Hiroshi A. Maeda. Evolutionary origin and functional diversification of aminotransferases. Journal of Biological Chemistry, 298:102122, Aug 2022. URL: https://doi.org/10.1016/j.jbc.2022.102122, doi:10.1016/j.jbc.2022.102122. This article has 104 citations and is from a domain leading peer-reviewed journal.
(binder2010branchedchainaminoacid pages 7-8): Stefan Binder. Branched-chain amino acid metabolism in arabidopsis thaliana. The Arabidopsis Book, 2010:e0137, Jan 2010. URL: https://doi.org/10.1199/tab.0137, doi:10.1199/tab.0137. This article has 313 citations and is from a peer-reviewed journal.
(niehaus2014arabidopsisandmaize pages 3-5): Thomas D. Niehaus, Thuy N.D. Nguyen, Satinder K. Gidda, Mona ElBadawi-Sidhu, Jennifer A. Lambrecht, Donald R. McCarty, Diana M. Downs, Arthur J.L. Cooper, Oliver Fiehn, Robert T. Mullen, and Andrew D. Hanson. arabidopsis and maize rida proteins preempt reactive enamine/imine damage to branched-chain amino acid biosynthesis in plastids. Jul 2014. URL: https://doi.org/10.1105/tpc.114.126854, doi:10.1105/tpc.114.126854. This article has 75 citations.
(niehaus2014arabidopsisandmaize pages 2-3): Thomas D. Niehaus, Thuy N.D. Nguyen, Satinder K. Gidda, Mona ElBadawi-Sidhu, Jennifer A. Lambrecht, Donald R. McCarty, Diana M. Downs, Arthur J.L. Cooper, Oliver Fiehn, Robert T. Mullen, and Andrew D. Hanson. arabidopsis and maize rida proteins preempt reactive enamine/imine damage to branched-chain amino acid biosynthesis in plastids. Jul 2014. URL: https://doi.org/10.1105/tpc.114.126854, doi:10.1105/tpc.114.126854. This article has 75 citations.
(niehaus2014arabidopsisandmaize pages 6-8): Thomas D. Niehaus, Thuy N.D. Nguyen, Satinder K. Gidda, Mona ElBadawi-Sidhu, Jennifer A. Lambrecht, Donald R. McCarty, Diana M. Downs, Arthur J.L. Cooper, Oliver Fiehn, Robert T. Mullen, and Andrew D. Hanson. arabidopsis and maize rida proteins preempt reactive enamine/imine damage to branched-chain amino acid biosynthesis in plastids. Jul 2014. URL: https://doi.org/10.1105/tpc.114.126854, doi:10.1105/tpc.114.126854. This article has 75 citations.
(niehaus2014arabidopsisandmaize pages 8-9): Thomas D. Niehaus, Thuy N.D. Nguyen, Satinder K. Gidda, Mona ElBadawi-Sidhu, Jennifer A. Lambrecht, Donald R. McCarty, Diana M. Downs, Arthur J.L. Cooper, Oliver Fiehn, Robert T. Mullen, and Andrew D. Hanson. arabidopsis and maize rida proteins preempt reactive enamine/imine damage to branched-chain amino acid biosynthesis in plastids. Jul 2014. URL: https://doi.org/10.1105/tpc.114.126854, doi:10.1105/tpc.114.126854. This article has 75 citations.
(koper2022evolutionaryoriginand pages 1-2): Kaan Koper, Sang-Woo Han, Delia Casas Pastor, Yasuo Yoshikuni, and Hiroshi A. Maeda. Evolutionary origin and functional diversification of aminotransferases. Journal of Biological Chemistry, 298:102122, Aug 2022. URL: https://doi.org/10.1016/j.jbc.2022.102122, doi:10.1016/j.jbc.2022.102122. This article has 104 citations and is from a domain leading peer-reviewed journal.