Novel Enzymatic Method for Imine Synthesis via the Oxidation of Primary Amines Using D-Amino Acid Oxidase from Porcine Kidney

Kawahara, Nobuhiro; Palasin, Kunwadee; Asano, Yasuhisa

doi:10.3390/catal12050511

Cited by 4 publications

(2 citation statements)

References 35 publications

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“…In P. aeruginosa, dadY is in an operon with dadA and dadX , which implicates DadY in alanine catabolism. DadA is an FAD-dependent dehydrogenase, the catalytic mechanism of which has been proposed to proceed through an imine intermediate, as demonstrated for other similar dehydrogenases [ 21 , 36 – 38 ]. Were this the case, the imine (imino-alanine, or 2-iminopropionate) released by DadA would be a potential substrate for DadY.…”

Section: Introductionmentioning

confidence: 92%

“…DadA cannot use oxygen as a terminal electron acceptor, distinguishing its mechanism from that of LOX and other oxidases [36]. The catalytic mechanism of DadA is thought to proceed via an imine intermediate, as is the case with similar enzymes [21,[36][37][38]. If generated, the imine intermediate would either remain in the active site of DadA or be released into the solvent prior to the deamination that results in pyruvate and ammonia.…”

Section: Dada Releases An Imine Substrate For Dadymentioning

confidence: 99%

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DadY (PA5303) is required for fitness of Pseudomonas aeruginosa when growth is dependent on alanine catabolism

Fulton¹,

Downs²

2022

Microb Cell

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Pseudomonas aeruginosa inhabits diverse environmental niches that can have varying nutrient composition. The ubiquity of this organism is facilitated by a metabolic strategy that preferentially utilizes low-energy, non-fermentable organic acids, such as amino acids, rather than the high-energy sugars preferred by many other microbes. The amino acid alanine is among the preferred substrates of P. aeruginosa. The dad locus encodes the constituents of the alanine catabolic pathway of P. aeruginosa. Physiological roles for DadR (AsnC-type transcriptional activator), DadX (alanine racemase), and DadA (D-amino acid dehydrogenase) have been defined in this pathway. An additional protein, PA5303, is encoded in the dad locus in P. aeruginosa. PA5303 is a member of the ubiquitous Rid protein superfamily and is desig-nated DadY based on the data presented herein. Despite its conservation in numerous Pseudomonas species and membership in the Rid superfamily, no physiological function has been assigned to DadY. In the present study, we demonstrate that DadA releases imino-alanine that can be deaminated by DadY in vitro. While DadY was not required for alanine catabolism in monoculture, dadY mutants had a dramatic fitness defect in competition with wildtype P. aeruginosa when alanine served as the sole carbon or nitrogen source. The data presented herein support a model in which DadY facilitates flux through the alanine catabolic pathway by removing the imine intermediate generated by DadA. Functional characterization of DadY contributes to our understanding of the role of the broadly conserved Rid family members.

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Section: Introductionmentioning

confidence: 92%

Section: Dada Releases An Imine Substrate For Dadymentioning

confidence: 99%

DadY (PA5303) is required for fitness of Pseudomonas aeruginosa when growth is dependent on alanine catabolism

Fulton¹,

Downs²

2022

Microb Cell

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Selective Synthesis of Imines via Oxidative Coupling of Primary Amines and Oxidation of Secondary Amines by Peroxides and other Competent Oxidants: A Short Review

Ravula,

Bandalla,

Dosarapu

et al. 2024

Orient. J. Chem

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Imines are certainly important constituents of many biomolecules, pharmaceuticals, agrochemicals, and fine chemicals. This review article highlights the standard protocols reported so far for the selective synthesis of imines via catalyzed and non-catalyzed (i) oxidative coupling of primary amines and (ii) oxidation of secondary amines in the presence of some competent/resourceful oxidants other than molecular O2 such as tert-butyl hydroperoxide (TBHP), H2O2, hypervalent iodines, persulfate, hypochlorite, electroactive species and graphene oxide. Indeed, the use of such oxidants offers a cost-effective experimental set-up, operational simplicity and also minimization of by-products. The cooperativity between catalyst, amine substrate, and oxidant is discussed in this review to understand the proposed mechanisms. Three consolidated data tables (Table 1, 2 & 3) are prepared to provide the summary of optimized reaction conditions (type of catalyst, type of oxidant, choice of solvent, amine-to-oxidant ratio, reaction time/temperature, conversion of amine, yield/selectivity of imine) of each article published to have a comparison.

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The Stability of Dimeric D-amino Acid Oxidase from Porcine Kidney Strongly Depends on the Buffer Nature and Concentration

2022

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The first step of the inactivation of the enzyme D-amino acid oxidase (DAAO) from porcine kidney at pH 5 and 7 is the enzyme subunit dissociation, while FAD dissociation has not a relevant role. At pH 9, both dissociation phenomena affect the enzyme stability. A strong effect of the buffer nature and concentration on enzyme stability was found, mainly at pH 7 and 9 (it was possible at the same temperature to have the enzyme fully inactivated in 5 mM of Hepes while maintaining 100% in 5 mM of glycine). The effect of the concentration of buffer on enzyme stability depended on the buffer: at pH 5, the acetate buffer had no clear effect, while Tris, Hepes and glycine (at pH 7) and carbonate (at pH 9) decreased enzyme stability when increasing their concentrations; phosphate concentration had the opposite effect. The presence of 250 mM of NaCl usually increased enzyme stability, but this did not occur in all cases. The effects were usually more significant when using low concentrations of DAAO and were not reverted upon adding exogenous FAD. However, when using an immobilized DAAO biocatalyst which presented enzyme subunits attached to the support, where dissociation was not possible, this effect of the buffer nature on enzyme stability almost disappeared. This suggested that the buffers were somehow altering the association/dissociation equilibrium of the enzyme.

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Novel Enzymatic Method for Imine Synthesis via the Oxidation of Primary Amines Using D-Amino Acid Oxidase from Porcine Kidney

Cited by 4 publications

References 35 publications

DadY (PA5303) is required for fitness of Pseudomonas aeruginosa when growth is dependent on alanine catabolism

DadY (PA5303) is required for fitness of Pseudomonas aeruginosa when growth is dependent on alanine catabolism

Selective Synthesis of Imines via Oxidative Coupling of Primary Amines and Oxidation of Secondary Amines by Peroxides and other Competent Oxidants: A Short Review

The Stability of Dimeric D-amino Acid Oxidase from Porcine Kidney Strongly Depends on the Buffer Nature and Concentration

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