CYP79B2

Existing Annotations Review

GO Term	Evidence	Action	Reason
GO:0002229 defense response to oomycetes	IGI PMID:20230487 Disease resistance of Arabidopsis to Phytophthora brassicae ...	KEEP AS NON CORE	Summary: The cyp79B2 cyp79B3 double mutant, which lacks IAOx and hence all IAOx-derived metabolites (indole glucosinolates and camalexin), is highly susceptible to the oomycete Phytophthora brassicae, whereas single pathway-branch mutants have only minor effects. Reason: Sound genetic evidence (IGI with CYP79B3) that CYP79B2/B3-derived indolic metabolites are needed for resistance to P. brassicae. CYP79B2 acts upstream by supplying the precursor IAOx; the antimicrobial work is done by downstream products (indole glucosinolate hydrolysis products and camalexin). Retain as a non-core, upstream physiological consequence of its catalytic role. Supporting Evidence: PMID:20230487 In contrast, the double mutant cyp79B2 cyp79B3, which has a blockage in the production of indole-3-aldoxime (IAOx), the common precursor of tryptophan-derived metabolites including camalexin and iGS, is highly susceptible to P. brassicae.
GO:0004497 monooxygenase activity	IEA GO_REF:0000120	KEEP AS NON CORE	Summary: Generic monooxygenase activity from InterPro/ARBA mapping of the cytochrome P450 domain. Reason: Correct but uninformative parent of the experimentally established tryptophan N-monooxygenase activity (GO:0090489), which captures the core activity. Retained as a true but non-core general term, consistent with the treatment of paralogous CYP79F1. Supporting Evidence: PMID:10922360 Heterologous expression of CYP79B2 in Escherichia coli shows that CYP79B2 catalyzes the conversion of tryptophan to indole-3-acetaldoxime.
GO:0005506 iron ion binding	IEA GO_REF:0000002	KEEP AS NON CORE	Summary: Iron ion binding inferred from P450 domain signatures; the heme iron is coordinated by the conserved Cys477 thiolate. Reason: CYP79B2 is a heme-thiolate P450; the iron is bound as part of the heme prosthetic group (C477A abolishes activity per UniProt). The term is correct as a cofactor description but is not the core function. Supporting Evidence: file:ARATH/CYP79B2/CYP79B2-deep-research-falcon.md The reaction required an NADPH–cytochrome-P450-reductase electron-transfer system in the reconstituted assays.
GO:0005783 endoplasmic reticulum	IBA GO_REF:0000033	ACCEPT	Summary: ER localization propagated across the CYP79/CYP71 clan P450 node; consistent with an N-terminal signal-anchor and with ER-like localization of CYP79B2-RFP colocalizing with ER-resident CYP71A13 in N. benthamiana. Reason: Plant A-type P450s are ER-anchored; the PAINT node placement is sound and is supported by direct colocalization data for CYP79B2 within the ER-associated camalexin metabolon (Mucha et al. 2019). Supporting Evidence: file:ARATH/CYP79B2/CYP79B2-deep-research-falcon.md CYP79B2–RFP displayed an ER-like reticulate pattern and colocalized with ER-localized CYP71A13–GFP PMID:31511315 We detected increased substrate affinity of CYP79B2 in the presence of CYP71A13, indicating an allosteric interaction.
GO:0006569 L-tryptophan catabolic process	IDA PMID:10681464 Arabidopsis cytochrome P450s that catalyze the first step of...	ACCEPT	Summary: Recombinant CYP79B2 converts L-tryptophan to indole-3-acetaldoxime, a reaction that consumes tryptophan. Reason: Conversion of Trp to IAOx is a catalytic step that removes tryptophan into secondary/hormone metabolism, so CYP79B2 directly executes a step of tryptophan catabolism as broadly defined. The more informative processes are indole glucosinolate and camalexin biosynthesis, but this term is not wrong. Supporting Evidence: PMID:10681464 We have identified two Arabidopsis cytochrome P450s (CYP79B2 and CYP79B3) that can convert Trp to indole-3-acetaldoxime (IAOx), a precursor to IAA and indole glucosinolates. PMID:10922360 Heterologous expression of CYP79B2 in Escherichia coli shows that CYP79B2 catalyzes the conversion of tryptophan to indole-3-acetaldoxime.
GO:0006952 defense response	IEP PMID:31568832 Translational Regulation of Metabolic Dynamics during Effect...	KEEP AS NON CORE	Summary: CYP79B2 is strongly induced at transcriptional and translational levels during RPS2-mediated effector-triggered immunity, and a cyp79B2 mutant shows reduced cell death. Reason: Expression evidence (plus a supporting mutant phenotype) linking CYP79B2 to defense; its contribution is through synthesis of camalexin precursor. Very general term; retained as non-core. Supporting Evidence: PMID:31568832 through the dramatic increases in both RS and RF (66 fold) of the key camalexin biosynthetic enzyme, tryptophan N-monooxygenase, CYP79B2 PMID:31568832 Indeed, the cyp79B2 mutant showed reduced PCD, indicating the importance of camalexin biosynthesis in this RPS2-mediated response (Figure S7C).
GO:0006952 defense response	IMP PMID:20023151 Tryptophan-derived metabolites are required for antifungal d...	KEEP AS NON CORE	Summary: Epistasis analysis with cyp79B2 cyp79B3 shows that indolic metabolites are required for mlo2-conditioned antifungal defense against powdery mildew and Botrytis. Reason: Genetic necessity of CYP79B2/B3-derived metabolites for antifungal defense; CYP79B2 acts upstream by producing IAOx. Retained as non-core; the core contribution is the biosynthetic step. Supporting Evidence: PMID:20023151 Results of genetic epistasis analysis suggest a decisive role for indolic metabolites in mlo2-conditioned antifungal defense against both biotrophic powdery mildews and a camalexin-sensitive strain of the necrotrophic fungus Botrytis cinerea.
GO:0006952 defense response	NAS PMID:31511315 The Formation of a Camalexin Biosynthetic Metabolon.	KEEP AS NON CORE	Summary: ComplexPortal statement that the camalexin metabolon (including CYP79B2) functions in defense. Reason: Camalexin is an antifungal phytoalexin, so the metabolon is defense-related, but the specific contribution of CYP79B2 is captured by camalexin biosynthetic process. Retained as a non-core general term. Supporting Evidence: PMID:31511315 Arabidopsis (Arabidopsis thaliana) efficiently synthesizes the antifungal phytoalexin camalexin without the apparent release of bioactive intermediates
GO:0009414 response to water deprivation	IEP PMID:23144921 Water stress and aphid feeding differentially influence meta...	MARK AS OVER ANNOTATED	Summary: CYP79B2 transcript decreased under drought stress in a single expression study. Reason: A single transcript change under drought does not indicate that CYP79B2 has a role in the response to water deprivation; no functional evidence links the enzyme to drought tolerance. Treated as over-annotation, consistent with the same row on CYP71B15/PAD3. Supporting Evidence: PMID:23144921 Transcript levels of the camalexin biosynthetic genes CYP79B2 and PAD3 were down-regulated by drought stress, resulting in less camalexin in plants under drought conditions than in plants under excessive water.
GO:0009507 chloroplast	ISM GO_REF:0000122	REMOVE	Summary: Chloroplast localization predicted by AtSubP sequence analysis. Reason: CYP79B2 is an N-terminally anchored ER P450 (signal-anchor TM 21-41) that colocalizes with ER-resident CYP71A13; there is no experimental support for plastid targeting. The prediction is a common mis-call for P450 N-terminal anchors. Supporting Evidence: file:ARATH/CYP79B2/CYP79B2-deep-research-falcon.md The early chloroplast assignment was sequence-based prediction only. file:ARATH/CYP79B2/CYP79B2-deep-research-falcon.md CYP79B2–RFP displayed an ER-like reticulate pattern and colocalized with ER-localized CYP71A13–GFP
GO:0009617 response to bacterium	IEP PMID:17573535 Arabidopsis cytochrome P450 monooxygenase 71A13 catalyzes th...	KEEP AS NON CORE	Summary: CYP79B2 expression responds to Pseudomonas syringae infection in the context of camalexin pathway induction (Nafisi et al. 2007). Reason: The cached record is abstract-only; the curator presumably saw expression data in the full text. CYP79B2 induction by bacteria is consistent with its role supplying IAOx for camalexin. Retained as non-core. Supporting Evidence: PMID:17573535 It is produced from Trp, which is converted to indole acetaldoxime (IAOx) by the action of cytochrome P450 monooxygenases CYP79B2 and CYP79B3.
GO:0009617 response to bacterium	IMP PMID:23073694 Metabolic and transcriptomic changes induced in Arabidopsis ...	KEEP AS NON CORE	Summary: cyp79B2 cyp79B3 mutants fail to mount Pseudomonas fluorescens SS101-induced resistance against Pst. Reason: Genetic requirement for IAOx-derived metabolites in a rhizobacterium-induced response; CYP79B2 acts upstream as a biosynthetic enzyme. Non-core. Supporting Evidence: PMID:23073694 Subsequent bioassays with seven Arabidopsis mutants ( myb51 , cyp79B2cyp79B3 , cyp81F2 , pen2 , cyp71A12 , cyp71A13 , and myb28myb29 ) disrupted in the biosynthesis pathways for these plant secondary metabolites showed that camalexin and glucosinolates are indeed required for the induction of Pst resistance by Pf .SS101 .
GO:0009625 response to insect	IEP PMID:23144921 Water stress and aphid feeding differentially influence meta...	KEEP AS NON CORE	Summary: Aphid (Myzus persicae) feeding increased CYP79B2 transcripts together with camalexin accumulation. Reason: Expression-based response; indole glucosinolates produced downstream of CYP79B2 are established anti-herbivore metabolites, so the response is biologically plausible but non-core. Supporting Evidence: PMID:23144921 persicae, increased expression of CYP79B2, CYP79B3, and PAD3 resulting in a 50 to 100-fold increase in the concentration of camalexin
GO:0009682 induced systemic resistance	IBA GO_REF:0000033	KEEP AS NON CORE	Summary: Induced systemic resistance propagated at a narrow CYP79B node (PTN008612649) containing CYP79B2 and CYP79B3. Reason: The node is the CYP79B subfamily and its experimental grounding is the CYP79B2/CYP79B3 mutant data (PMID:23073694); the target appearing among the sources is expected. The term reflects an upstream requirement for IAOx-derived defense metabolites rather than the enzymatic function, so it is kept as non-core. Supporting Evidence: PMID:23073694 Subsequent bioassays with seven Arabidopsis mutants ( myb51 , cyp79B2cyp79B3 , cyp81F2 , pen2 , cyp71A12 , cyp71A13 , and myb28myb29 ) disrupted in the biosynthesis pathways for these plant secondary metabolites showed that camalexin and glucosinolates are indeed required for the induction of Pst resistance by Pf .SS101 .
GO:0009682 induced systemic resistance	IMP PMID:23073694 Metabolic and transcriptomic changes induced in Arabidopsis ...	KEEP AS NON CORE	Summary: Rhizobacterium (P. fluorescens SS101)-induced systemic resistance to Pst requires CYP79B2/B3-dependent camalexin and glucosinolates. Reason: Experimental support for necessity of CYP79B2/B3 products in ISR; the enzyme acts upstream by producing IAOx. Non-core. Supporting Evidence: PMID:23073694 Subsequent bioassays with seven Arabidopsis mutants ( myb51 , cyp79B2cyp79B3 , cyp81F2 , pen2 , cyp71A12 , cyp71A13 , and myb28myb29 ) disrupted in the biosynthesis pathways for these plant secondary metabolites showed that camalexin and glucosinolates are indeed required for the induction of Pst resistance by Pf .SS101 .
GO:0009684 indoleacetic acid biosynthetic process	IMP PMID:15772288 Sites and regulation of auxin biosynthesis in Arabidopsis ro...	KEEP AS NON CORE	Summary: IAA synthesis rate is reduced in roots of the cyp79B2 cyp79B3 double mutant; both genes are expressed at sites of high IAA synthesis. Reason: CYP79B2 makes IAOx, which can be converted to IAA via IAN, so it does catalyse an early step of one (minor, Brassicales-specific) Trp-dependent IAA route. Its contribution is conditional and quantitatively small relative to the TAA1/YUCCA pathway, so the term is retained as non-core. Supporting Evidence: PMID:15772288 Root-localized IAA synthesis was diminished in a cyp79B2 cyp79B3 double knockout, suggesting an important role for Trp-dependent IAA synthesis pathways in the root. PMID:12464638 Conversely, cyp79B2 cyp79B3 double mutants have reduced levels of IAA and show growth defects consistent with partial auxin deficiency.
GO:0010120 camalexin biosynthetic process	NAS PMID:31511315 The Formation of a Camalexin Biosynthetic Metabolon.	ACCEPT	Summary: CYP79B2 is a member of the camalexin biosynthetic metabolon and catalyses its first step (Trp to IAOx). Reason: CYP79B2 catalyses the first step of camalexin biosynthesis; the cyp79B2 cyp79B3 double mutant is devoid of camalexin and labeled IAOx is incorporated into camalexin. CYP79B2 physically associates with downstream CYP71A13/CYP71B15. This is a direct catalytic participation, not mere necessity. Supporting Evidence: PMID:15148388 We show that camalexin, the indole phytoalexin of Arabidopsis thaliana, is synthesized from tryptophan via indole-3-acetaldoxime (IAOx) in a reaction catalyzed by CYP79B2 and CYP79B3. PMID:31511315 We detected increased substrate affinity of CYP79B2 in the presence of CYP71A13, indicating an allosteric interaction.
GO:0010120 camalexin biosynthetic process	TAS PMID:16167893 Secondary metabolites influence Arabidopsis/Botrytis interac...	ACCEPT	Summary: Traceable author statement on camalexin production by CYP79B2-dependent pathway in Arabidopsis/Botrytis interactions. Reason: The cited paper (abstract-only in cache) uses camalexin-deficient genotypes; the underlying claim that CYP79B2 catalyses the first step of camalexin biosynthesis is well established (Glawischnig et al. 2004). Supporting Evidence: PMID:16167893 Botrytis cinerea isolates showed differing sensitivity to purified camalexin, and camalexin-sensitive isolates produced larger lesions on camalexin-deficient Arabidopsis genotypes than on the wild type. PMID:15148388 We show that camalexin, the indole phytoalexin of Arabidopsis thaliana, is synthesized from tryptophan via indole-3-acetaldoxime (IAOx) in a reaction catalyzed by CYP79B2 and CYP79B3.
GO:0016020 membrane	IBA GO_REF:0000033	MODIFY	Summary: Membrane localization propagated at the P450 node. Reason: CYP79B2 is a single-pass, signal-anchored membrane protein, so the term is correct, but the experimentally supported membrane is the ER (CYP79B2-RFP colocalizes with ER-resident CYP71A13); endoplasmic reticulum membrane is the precise term, consistent with the ER IBA from the same node. Propagation Review Root cause: NO FAILURE CORE Sources checked: PANTHER:PTN001210282 · PTN001210282 SUPPORTS TRANSFER Membrane anchoring is conserved across this P450 node and CYP79B2 is inside the clade; the MODIFY only sharpens the term to ER membrane, it does not dispute the transfer. Proposed replacements: endoplasmic reticulum membrane Supporting Evidence: file:ARATH/CYP79B2/CYP79B2-deep-research-falcon.md CYP79B2–RFP displayed an ER-like reticulate pattern and colocalized with ER-localized CYP71A13–GFP
GO:0016020 membrane	IEA GO_REF:0000044	MODIFY	Summary: Membrane from UniProt subcellular location (single-pass membrane protein). Reason: Correct but non-specific; the experimentally supported location is the ER (CYP79B2-RFP colocalizes with ER-resident CYP71A13), so endoplasmic reticulum membrane is the appropriate term. Proposed replacements: endoplasmic reticulum membrane Supporting Evidence: file:ARATH/CYP79B2/CYP79B2-deep-research-falcon.md CYP79B2–RFP displayed an ER-like reticulate pattern and colocalized with ER-localized CYP71A13–GFP
GO:0016020 membrane	NAS PMID:31511315 The Formation of a Camalexin Biosynthetic Metabolon.	MODIFY	Summary: ComplexPortal: the camalexin metabolon assembles on membranes. Reason: The metabolon assembles at the ER surface; endoplasmic reticulum membrane is the more precise location for CYP79B2. Proposed replacements: endoplasmic reticulum membrane Supporting Evidence: file:ARATH/CYP79B2/CYP79B2-deep-research-falcon.md CYP79B2–RFP displayed an ER-like reticulate pattern and colocalized with ER-localized CYP71A13–GFP
GO:0016705 oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen	IEA GO_REF:0000120	KEEP AS NON CORE	Summary: General paired-donor oxygenase term from P450 domain mapping. Reason: True ancestor of tryptophan N-monooxygenase activity (GO:0090489) but uninformative; retained as non-core. Supporting Evidence: PMID:10922360 Heterologous expression of CYP79B2 in Escherichia coli shows that CYP79B2 catalyzes the conversion of tryptophan to indole-3-acetaldoxime.
GO:0016709 oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, NAD(P)H as one donor, and incorporation of one atom of oxygen	IBA GO_REF:0000033	MODIFY	Summary: Paired-donor monooxygenase with NAD(P)H as one donor, propagated at the P450 node PTN001210282. Reason: The general P450 monooxygenase function at this node is sound, but microsomal P450s such as CYP79B2 receive electrons from NADPH via NADPH-cytochrome P450 reductase (a flavoprotein); the Rhea reaction (RHEA:33279) uses reduced [NADPH--hemoprotein reductase]. In GO, tryptophan N-monooxygenase activity is_a GO:0016712 (reduced flavin or flavoprotein as one donor), not GO:0016709. Replace with GO:0016712, as done for paralogous CYP79F1. Propagation Review Root cause: TERM SCOPING PROBLEM Sources checked: PANTHER:PTN001210282 · PTN001210282 SUPPORTS TRANSFER The P450 monooxygenase function at this node is sound and CYP79B2 is inside the clade; only the electron-donor branch of the asserted term (NAD(P)H rather than flavoprotein reductase) is mis-scoped for microsomal P450s. Proposed replacements: oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, reduced flavin or flavoprotein as one donor, and incorporation of one atom of oxygen Supporting Evidence: file:ARATH/CYP79B2/CYP79B2-deep-research-falcon.md The reaction required an NADPH–cytochrome-P450-reductase electron-transfer system in the reconstituted assays. file:ARATH/CYP79B2/CYP79B2-uniprot.txt Reaction=L-tryptophan + 2 reduced [NADPH--hemoprotein reductase] + 2 O2
GO:0020037 heme binding	IEA GO_REF:0000002	KEEP AS NON CORE	Summary: Heme binding from P450 domain signatures. Reason: CYP79B2 is a heme-thiolate P450 (Cys477 axial ligand; C477A abolishes activity). The cofactor-binding term is correct but not the core function. Supporting Evidence: file:ARATH/CYP79B2/CYP79B2-deep-research-falcon.md The reaction required an NADPH–cytochrome-P450-reductase electron-transfer system in the reconstituted assays.
GO:0042742 defense response to bacterium	IMP PMID:19095898 Glucosinolate metabolites required for an Arabidopsis innate...	KEEP AS NON CORE	Summary: cyp79B2 cyp79B3 plants, lacking indole glucosinolates, are impaired in flg22-induced callose and in glucosinolate-dependent restriction of bacterial growth (Clay et al. 2009). Reason: Genetic necessity of CYP79B2/B3 for an antibacterial response mediated by indole glucosinolate breakdown products (CYP81F2/PEN2 pathway). CYP79B2 acts upstream as the first biosynthetic enzyme. Non-core. Supporting Evidence: PMID:19095898 The IGS biosynthetic double mutant cyp79B2 cyp79B3, which completely lacks IGS (21), as well as mutants atr4-1/cyp83B1 and ugt74B1-2, were impaired in the induction of the callose response
GO:0044272 sulfur compound biosynthetic process	IEA GO_REF:0000117	MODIFY	Summary: Sulfur compound biosynthetic process from an ARBA rule, reflecting the CYP79 role in glucosinolate synthesis. Reason: CYP79B2 catalyses the first committed step of indole glucosinolate biosynthesis (Trp to IAOx; the double mutant completely lacks indole glucosinolates, and overexpression raises them). The specific term is indole glucosinolate biosynthetic process, which is_a sulfur compound biosynthetic process. Comparator check: the next enzyme, CYP83B1, carries GO:0009759 (IDA), so the term is applied to the catalysing enzymes of this pathway. Proposed replacements: indole glucosinolate biosynthetic process Supporting Evidence: PMID:10922360 Arabidopsis overexpressing CYP79B2 has increased levels of indole glucosinolates, which strongly indicates that CYP79B2 is involved in indole glucosinolate biosynthesis. PMID:15148388 These results demonstrate that only CYP79B2 and CYP79B3 contribute significantly to the IAOx pool from which camalexin and indole glucosinolates are synthesized.
GO:0052544 defense response by callose deposition in cell wall	IMP PMID:19095898 Glucosinolate metabolites required for an Arabidopsis innate...	KEEP AS NON CORE	Summary: The cyp79B2 cyp79B3 double mutant is impaired in flg22-induced callose deposition. Reason: CYP79B2 does not deposit callose; it supplies IAOx for indole glucosinolate synthesis, whose 4-methoxy derivative is hydrolysed by PEN2 to signal callose deposition. The requirement is genuine but indirect and context-dependent (Schlaeppi et al. 2010 found wild-type-like callose in cyp79B2 cyp79B3 challenged with P. brassicae). Kept as a non-core upstream annotation. Supporting Evidence: PMID:19095898 The IGS biosynthetic double mutant cyp79B2 cyp79B3, which completely lacks IGS (21), as well as mutants atr4-1/cyp83B1 and ugt74B1-2, were impaired in the induction of the callose response PMID:20230487 we concluded that the lack of IAOx-derived compounds renders Arabidopsis susceptible despite wild-type-like pathogen-induced hypersensitive cell death, stress hormone signaling and callose deposition
GO:0090489 tryptophan N-monooxygenase activity	EXP PMID:10681464 Arabidopsis cytochrome P450s that catalyze the first step of...	ACCEPT	Summary: Recombinant CYP79B2 converts L-tryptophan to indole-3-acetaldoxime (EC 1.14.14.156); confirmed independently by Mikkelsen et al. 2000 (Km 21 uM). Reason: This is the defining catalytic activity of CYP79B2, demonstrated by two independent heterologous expression studies, with no oxime formation from Phe or Tyr. Supporting Evidence: PMID:10681464 We have identified two Arabidopsis cytochrome P450s (CYP79B2 and CYP79B3) that can convert Trp to indole-3-acetaldoxime (IAOx), a precursor to IAA and indole glucosinolates. PMID:10922360 Heterologous expression of CYP79B2 in Escherichia coli shows that CYP79B2 catalyzes the conversion of tryptophan to indole-3-acetaldoxime.
GO:0090489 tryptophan N-monooxygenase activity	IEA GO_REF:0000120	ACCEPT	Summary: Tryptophan N-monooxygenase activity from Rhea/EC mapping. Reason: Consistent with the experimentally established activity. Supporting Evidence: PMID:10922360 Heterologous expression of CYP79B2 in Escherichia coli shows that CYP79B2 catalyzes the conversion of tryptophan to indole-3-acetaldoxime.
GO:1902494 catalytic complex	NAS PMID:31511315 The Formation of a Camalexin Biosynthetic Metabolon.	KEEP AS NON CORE	Summary: ComplexPortal camalexin metabolon (CPX-2833) includes CYP79B2 with CYP71A13, CYP71B15, ATR1 and GSTU4. Reason: Co-IP and FRET-FLIM support association of CYP79B2 with the downstream camalexin P450s, and CYP71A13 increases the substrate affinity of CYP79B2. The metabolon is a transient enzyme assembly; catalytic complex is a generic term. Retained as non-core. Supporting Evidence: PMID:31511315 determined that the camalexin biosynthetic P450 enzymes copurified with these enzymes. PMID:31511315 We detected increased substrate affinity of CYP79B2 in the presence of CYP71A13, indicating an allosteric interaction.

Gene Description

Existing Annotations Review

Core Functions

ER-anchored tryptophan N-monooxygenase that converts L-tryptophan to indole-3-acetaldoxime (IAOx), the first committed step shared by indole glucosinolate and camalexin biosynthesis (redundantly with CYP79B3).

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