Characterization of Nα-benzyloxycarbonyl-l-lysine oxidizing enzyme from Rhodococcus sp. AIU Z-35-1

Isobe, Kimiyasu; Nagasawa, Shouko

doi:10.1263/jbb.104.218

Cited by 19 publications

(17 citation statements)

References 13 publications

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“…Thus, it was presumed that one product from l -citrulline is 2-oxo-5-ureidovaleric acid and the other is pyrrolidine-1-carbamyl-2-hydroxy-2-carboxylic acid. These results experimentally supported our previous report that l -AAO from Rhodococcus Z-35-1 is l -specific amino acid oxidase with broad substrate specificity [16]. They also indicate that the above l -amino acids were converted to the corresponding α -keto-acids by the oxidative deamination of the α -amino group of l -amino acids.…”

Section: Resultssupporting

confidence: 91%

“…The l -AAO from Rhodoccocus sp. Z-35-1 was purified according to our method described in a previous report [16]. …”

Section: Methodsmentioning

confidence: 99%

“…AIU Z-35-1, for production of N α -benzyloxycarbonyl- l -aminoadipic acid ( N α -Z- l -AAA) from N α -benzyloxycarbonyl- l -lysine ( N α -Z- l -lysine) [15]. In the analysis of this reaction, it was demonstrated that N α -Z- l -lysine was converted to N α -Z- l -AAA via N α -benzyloxycarbonyl- l -aminoadipate- δ -semialdehyde ( N α -Z- l -AASA), and the conversion of N α -Z- l -lysine into N α -Z- l -AASA was catalyzed by a l -specific amino acid oxidase ( l -AAO) with broad substrate specificity [16]. Thus, the l -AAO catalyzed an oxidative deamination of N α -acyl- l -lysine, N ε -acyl- l -lysine, l -lysine and many other l -amino acids, but not of N α -acyl- d -lysine, N ε -acyl- d -lysine and d -amino acids.…”

Section: Introductionmentioning

confidence: 99%

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A Simple Enzymatic Method for Production of a Wide Variety of D-Amino Acids Using L-Amino Acid Oxidase from Rhodococcus sp. AIU Z-35-1

et al. 2010

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A simple enzymatic method for production of a wide variety of D-amino acids was developed by kinetic resolution of DL-amino acids using L-amino acid oxidase (L-AAO) with broad substrate specificity from Rhodococcus sp. AIU Z-35-1. The optimum pH of the L-AAO reaction was classified into three groups depending on the L-amino acids as substrate, and their respective activities between pH 5.5 and 8.5 accounted for more than 60% of the optimum activity. The enzyme was stable in the range from pH 6.0 to 8.0, and approximately 80% of the enzyme activity remained after incubation at 40°C for 60 min at pH 7.0. D-Amino acids such as D-citrulline, D-glutamine, D-homoserine or D-arginine, which are not produced by D-aminoacylases or D-hydantoinases, were produced from the racemic mixture within a 24-hr reaction at 30°C and pH 7.0. Thus, the present method using L-AAO was versatile for production of a wide variety of D-amino acids.

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Section: Resultssupporting

confidence: 91%

“…The l -AAO from Rhodoccocus sp. Z-35-1 was purified according to our method described in a previous report [16]. …”

Section: Methodsmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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A Simple Enzymatic Method for Production of a Wide Variety of D-Amino Acids Using L-Amino Acid Oxidase from Rhodococcus sp. AIU Z-35-1

et al. 2010

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“…This activity had never been described in other LAOs, which undergo deamination at the alpha ƒngroup. The only similar activity described so far is an LAO with a broad substrate range from Rhodococcus sp., which oxidizes the ɛ position of l -lysine when the alpha is blocked [134]. Thus, l -lysine-ɛ-oxidase synthesized by M. mediterranea received a new number from the Enzyme Commission (E.C.…”

Section: L-amino Acid Oxidasesmentioning

confidence: 99%

Finding New Enzymes from Bacterial Physiology: A Successful Approach Illustrated by the Detection of Novel Oxidases in Marinomonas mediterranea

2010

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The identification and study of marine microorganisms with unique physiological traits can be a very powerful tool discovering novel enzymes of possible biotechnological interest. This approach can complement the enormous amount of data concerning gene diversity in marine environments offered by metagenomic analysis, and can help to place the activities associated with those sequences in the context of microbial cellular metabolism and physiology. Accordingly, the detection and isolation of microorganisms that may be a good source of enzymes is of great importance. Marinomonas mediterranea, for example, has proven to be one such useful microorganism. This Gram-negative marine bacterium was first selected because of the unusually high amounts of melanins synthesized in media containing the amino acid l-tyrosine. The study of its molecular biology has allowed the cloning of several genes encoding oxidases of biotechnological interest, particularly in white and red biotechnology. Characterization of the operon encoding the tyrosinase responsible for melanin synthesis revealed that a second gene in that operon encodes a protein, PpoB2, which is involved in copper transfer to tyrosinase. This finding made PpoB2 the first protein in the COG5486 group to which a physiological role has been assigned. Another enzyme of interest described in M. mediterranea is a multicopper oxidase encoding a membrane-associated enzyme that shows oxidative activity on a wide range of substrates typical of both laccases and tyrosinases. Finally, an enzyme very specific for l-lysine, which oxidises this amino acid in epsilon position and that has received a new EC number (1.4.3.20), has also been described for M. mediterranea. Overall, the studies carried out on this bacterium illustrate the power of exploring the physiology of selected microorganisms to discover novel enzymes of biotechnological relevance.

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“…5 More recently, Rhodococcus sp. AIU Z-35-1 LAAO has been employed for the resolution of D,L-mixtures of citrulline, Gln, homoserine, N-ε-acety-Lys and Arg, 6 and crude extracts of A. fumigatus have been used for the racemic resolution of Ala, Phe and Tyr: nevertheless, an optically pure product was obtained only for D-Ala. 7 LAAO from the bacterium R. opacus DSM 43250 was also used for the racemic resolution of 7 mM D,L-Phe and D,L-Leu and 3,4-dihydroxyphenyl-L-alanine (L-DOPA), the precursor of the melanine pigment, of all cathecolamine neurotransmitters, and of hormones and one of the main drugs for treatment of Parkinson's disease. By employing a batch biotransformation based on a membrane reactor, complete oxidation of L-DOPA was reached for three consecutive cycles performed by adding fresh L-DOPA to the same reaction mixture without discharge of the products.…”

Section: Introductionmentioning

confidence: 99%

Immobilization of l-aspartate oxidase from Sulfolobus tokodaii as a biocatalyst for resolution of aspartate solutions

D’Arrigo

Allegretti

Fiorati

et al. 2015

Catal. Sci. Technol.

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L-Aspartate oxidase from the thermophilic archaebacterium Sulfolobus tokodaii (StLASPO) catalyzes the stereoselective oxidative deamination of L-aspartate to yield oxaloacetate, ammonia and hydrogen peroxide. The recombinant flavoenzyme shows distinctive features that make it attractive for biotechnological applications (it is highly thermostable, it is stable in a broad pH range, it tightly binds the FAD cofactor and it shows a low K m for dioxygen). In order to set up an efficient and economically feasible bioconversion process, in this work, we investigated the immobilization of this novel biocatalyst. The best results in terms of immobilization yield have been obtained when StLASPO was immobilized on the amino support Relizyme™ HA403/S R after activation with glutaraldehyde and on the epoxy support SEPABEADS® EC-EP/S (in both cases, through the free amino groups of the enzyme), as well as prepared as cross-linked enzyme aggregates (CLEA). By using the Relizyme™ HA403/S R support, as well as by the CLEA preparation procedure, full immobilization in terms of enzymatic activity was obtained. Immobilized StLASPO was used for the resolution of racemic solutions of 50 mM D,L-aspartate achieving full resolution in <1 hour. Indeed, the Relizyme-StLASPO immobilized enzyme (the one showing the highest immobilization yield) was efficiently reused in 5 cycles keeping full oxidation of L-aspartate in ≤2 hours. In a semi-preparative scale reaction, 66 mg of enantiomerically pure D-aspartate were produced in 1 day using 20 units of enzyme.

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Characterization of Nα-benzyloxycarbonyl-l-lysine oxidizing enzyme from Rhodococcus sp. AIU Z-35-1

Cited by 19 publications

References 13 publications

A Simple Enzymatic Method for Production of a Wide Variety of D-Amino Acids Using L-Amino Acid Oxidase from Rhodococcus sp. AIU Z-35-1

A Simple Enzymatic Method for Production of a Wide Variety of D-Amino Acids Using L-Amino Acid Oxidase from Rhodococcus sp. AIU Z-35-1

Finding New Enzymes from Bacterial Physiology: A Successful Approach Illustrated by the Detection of Novel Oxidases in Marinomonas mediterranea

Immobilization of l-aspartate oxidase from Sulfolobus tokodaii as a biocatalyst for resolution of aspartate solutions

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