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Aminotransferase

Aminotransferase involved in local and systemic acquired resistance (SAR) to the bacterial pathogen P.syringae. Required for salicylic acid (SA) and camalexin accumulation upon pathogen infection. Possesses aminotransferase activity in vitro and may generate amino-acid-derived defense signals in vivo. May be involved in ethylene-induced senescence signaling.

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Aminotransferase ALD1

Also known as Aminotransferase ALD1 (AGD2-like defense response protein 1).
Aminotransferase involved in local and systemic acquired resistance (SAR) to the bacterial pathogen P.syringae. Required for salicylic acid (SA) and camalexin accumulation upon pathogen infection. Possesses aminotransferase activity in vitro and may generate amino-acid-derived defense signals in vivo. May be involved in ethylene-induced senescence signaling.

Aminotransferase apf4

Also known as Aminotransferase apf4 (Apicidin F synthesis protein 4).
Aminotransferase; part of the gene cluster that mediates the biosynthesis of the cyclic tetrapeptide apicidin F (APF) (PubMed:25058475). The non-ribosomal peptide synthetase apf1 incorporates four different amino acids to produce apicidin F: L-phenylalanine, D-pipecolic acid (D-pip), N-methoxy-L-tryptophan and L-2-aminooctanedioic acid (PubMed:25058475). L-Phenylalanine is the only proteinogenic amino acid directly used by apf1 (PubMed:24195442, PubMed:25058475). The 3 other apf1 substrates are non-proteinogenic and have to be modified by other enzymes of the cluster (PubMed:25058475). Lysine is converted to delta-1-pyrroline-5-carboxylate (P5C) which is reduced to L-pipecolic acid (L-pip) by apf3 (PubMed:25058475). L-pip is epimerized to D-pip, probably by apf1 activity, prior to incorporation (PubMed:25058475). L-Tryptophan is N-oxidyzed by one of the cytochrome P450 monooxygenases (apf7 or apf8), and further methylated at the hydroxy group by the O-methyltransferase apf6 to yield N-methoxy-L-tryptophan (PubMed:25058475). The synthesis of the fourth apf1 substrate is more complex (PubMed:25058475). The fatty acid synthase apf5 is involved in the synthesis of the octanoic acid backbone of L-2-aminooctanedioic acid by fixing one acetyl-CoA unit and three malonyl-CoA units (PubMed:25058475). Then one of the cytochrome P450 monooxygenases (apf7 or apf8) may oxidize this backbone to 2-oxooctanoic acid (PubMed:25058475). The aminotransferase apf4 is predicted to catalyze the exchange of the keto group with an amino group (PubMed:25058475). The next step would be the oxidation of 2-aminooctanoic acid by one of the cytochrome P450 monooxygenases (apf7 or apf8). The last step is the oxidation of 2-amino-8-hydroxyoctanoic acid to 2-aminooctanedioic acid is catalyzed by the FAD-dependent monooxygenase apf9 (PubMed:25058475).

Aminotransferase PigE

Involved in the biosynthesis of 2-methyl-3-n-amyl-pyrrole (MAP), one of the terminal products involved in the biosynthesis of the red antibiotic prodigiosin (Pig). Catalyzes the transamination to the aldehyde group of 3-acetyloctanal, resulting in an aminoketone, which spontaneously cyclizes to yield the dihydro form of MAP (H2MAP).

Aminotransferase tdiD

Also known as Aminotransferase tdiD (Terrequinone biosynthesis protein D).
Aminotransferase; part of the gene cluster that mediates the biosynthesis of terrequinone A, an antitumor agent (PubMed:17704773, PubMed:16426969, PubMed:17291795, PubMed:22083274). The first step in the biosynthetic pathway for terrequinone A is formation of indole pyruvic acid (IPA) from L-tryptophan by the aminotransferase tdiD (PubMed:17704773). TdiA then immediately converts unstable IDA to didemethylasterriquinone D (DDAQ D) (PubMed:17704773). TdiB then catalyzes reverse prenylation by transfering dimethylallyl diphosphate to carbon atom 2' of DDAQ D, to yield asterriquinone C-1 (PubMed:18029206). Finally, tdiC and tdiE enzymes robustly convert asterriquinone C-1 to terrequinone A via a transformation involving regular prenylation at carbon atom 5, which requires elimination of the hydroxy group on C-5 (PubMed:17704773, PubMed:18029206).

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