Purification and characterization of an l-amino acid oxidase from Pseudomonas sp. AIU 813

Isobe, Kimiyasu; Sugawara, Asami; Domon, Hanako; Fukuta, Yasuhisa; Asano, Yasuhisa

doi:10.1016/j.jbiosc.2012.04.020

Cited by 25 publications

(18 citation statements)

References 21 publications

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“…An l ‐AAO from Pseudomonas sp. AIU 813 was found to be specific to l ‐lysine, l ‐ornithine and l ‐arginine [11]. In the microbial l ‐AAOs, which are specific to these basic amino acids, the l ‐AAO from Trichoderma viride [12] and Trichoderma sp.…”

Section: Introductionmentioning

confidence: 99%

Mutational and crystallographic analysis of l‐amino acid oxidase/monooxygenase from Pseudomonas sp. AIU 813: Interconversion between oxidase and monooxygenase activities

Matsui

Sugawara

et al. 2014

FEBS Open Bio

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Section: Introductionmentioning

confidence: 99%

Mutational and crystallographic analysis of l‐amino acid oxidase/monooxygenase from Pseudomonas sp. AIU 813: Interconversion between oxidase and monooxygenase activities

Matsui

Sugawara

et al. 2014

FEBS Open Bio

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“…Since enzyme I had the lowest K m value for 4-ABAD among these three enzymes, we applied it to an L-lysine assay by coupling it with L-amino acid oxidase/monooxygenase (L-AAO/MOG) from Pseudomonas sp. AIU 813 (6). We then further purified the other two enzymes and revealed certain properties of both.…”

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confidence: 98%

Characterization of two amine oxidases from Aspergillus carbonarius AIU 205

Sugawara

Matsui

Yamada

et al. 2015

Journal of Bioscience and Bioengineering

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“…AIU 813 ( l ‐AAO/MOG) is a bifunctional enzyme that exhibits both the l ‐Lys α‐oxidase and l ‐Lys 2‐monooxygenase (EC http://www.chem.qmul.ac.uk/iubmb/enzyme/EC1/13/12/2.html) activities (Fig. ) . Most l ‐AAOs show a wide range of substrate specificity, as represented by snake venom l ‐AAOs .…”

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confidence: 99%

“…l ‐AAO/MOG shows limited substrate specificity toward l ‐amino acids with a positively charged side chain group. Relative oxidase activities of l ‐AAO/MOG toward l ‐ornithine (Orn) and l ‐Arg compared with l ‐Lys were 31% and 6%, respectively . In our previous study , a ligand‐free crystal structure of l ‐AAO/MOG and its interconversion between oxidase and monooxygenase activities by chemical modification and point mutation were described.…”

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Ligand complex structures of l‐amino acid oxidase/monooxygenase from Pseudomonas sp. AIU 813 and its conformational change

Matsui

Arakawa

et al. 2018

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l ‐Amino acid oxidase/monooxygenase from Pseudomonas sp. AIU 813 ( l ‐ AAO / MOG ) catalyzes both the oxidative deamination and oxidative decarboxylation of the α‐group of l ‐Lys to produce a keto acid and amide, respectively. l ‐ AAO / MOG exhibits limited specificity for l ‐amino acid substrates with a basic side chain. We previously determined its ligand‐free crystal structure and identified a key residue for maintaining the dual activities. Here, we determined the structures of l ‐ AAO / MOG complexed with l ‐Lys, l ‐ornithine, and l ‐Arg and revealed its substrate recognition. Asp238 is located at the ceiling of a long hydrophobic pocket and forms a strong interaction with the terminal, positively charged group of the substrates. A mutational analysis on the D238A mutant indicated that the interaction is critical for substrate binding but not for catalytic control between the oxidase/monooxygenase activities. The catalytic activities of the D238E mutant unexpectedly increased, while the D238F mutant exhibited altered substrate specificity to long hydrophobic substrates. In the ligand‐free structure, there are two channels connecting the active site and solvent, and a short region located at the dimer interface is disordered. In the l ‐Lys complex structure, a loop region is displaced to plug the channels. Moreover, the disordered region in the ligand‐free structure forms a short helix in the substrate complex structures and creates the second binding site for the substrate. It is assumed that the amino acid substrate enters the active site of l ‐ AAO / MOG through this route. Database The atomic coordinates and structure factors (codes 5YB6 , 5YB7 , and 5YB8 ) have been deposited in the Protein Data Bank ( http://wwpdb.org/ ). EC numbers 1.4.3.2 ( l ‐amino acid oxidase), 1.13.12.2 (lysine 2‐monooxygenase).

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Purification and characterization of an l-amino acid oxidase from Pseudomonas sp. AIU 813

Cited by 25 publications

References 21 publications

Mutational and crystallographic analysis of l‐amino acid oxidase/monooxygenase from Pseudomonas sp. AIU 813: Interconversion between oxidase and monooxygenase activities

Mutational and crystallographic analysis of l‐amino acid oxidase/monooxygenase from Pseudomonas sp. AIU 813: Interconversion between oxidase and monooxygenase activities

Characterization of two amine oxidases from Aspergillus carbonarius AIU 205

Ligand complex structures of l‐amino acid oxidase/monooxygenase from Pseudomonas sp. AIU 813 and its conformational change

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