Function of the Arginine Oxygenase Pathway in Utilization of<scp>L</scp>-Arginine-related Compounds in<i>Arthrobacter globiformis</i>and<i>Brevibacterium helvolum</i>

Kaneoke, Mitsuoki; Shiota, Kazuma; Kusunose, Masahiro; Shimizu, Eiichi; Yorifuji, Tohru

doi:10.1271/bbb.57.814

Cited by 5 publications

(3 citation statements)

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“…The most noticeable feature of N. simplex is that agmatine, carbamoylputrescine, and putrescine are degraded in a manner which is quite different from that found in A. globiformis and B. helvolum. 8 ) Figure 4 illustrates the pathways in N. simplex that we propose. In A. globiformis and B. helvolum, agmatine deiminase, carbamoylputrescine hydrolase, and putrescine oxidase are involved in the degradation of agmatine and the related compounds to 4-aminobutyrate.…”

Section: Dehydrogenase Activities Acting On Aminotransferase Reactionmentioning

confidence: 99%

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Metabolism ofL-Arginine, Agmatine, and Related Compounds inNocardioides simplex

Kaneoke

Shimizu

Yorifuji

1994

Bioscience, Biotechnology, and Biochemistry

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Nocardioides simplex IFO 12069 (Arthrobacter simplex ATCC 6946) was examined for the degradation of L-ornithine, L-citrulline, L-arginine, D-arginine, agmatine, carbamoylputrescine, and putrescine, and the results were compared with those obtained in a previous study with A. globiformis and Brevibacterium helvolum. D-Arginine as well as L-arginine was degraded via the arginine oxygenase pathway. A part of L-citrulline was probably degraded via the pathway. The L-ornithine degradation via the pathway was obscure. Guanidinobutyrase was induced by agmatine, which was shown to be degraded via a unique pathway. The first step of the pathway converted agmatine to 4-guanidinobutyraldehyde by transferring the amino group to pyruvate. The second step was the NAD-Iinked dehydrogenation of the aldehyde to 4-guanidinobutyrate, which was then degraded to 4-aminobutyrate. The enzymes for the first and second steps were identified as diaminopropane aminotransferase (EC 2.6.1.-) and aminobutyraldehyde dehydrogenase (EC 1.2.1.19), respectively. These enzymes also degraded putrescine to 4-aminobutyrate. Carbamoylputrescine was converted by the aminotransferase to the corresponding aldehyde, which was accumulated in the medium.

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Section: Dehydrogenase Activities Acting On Aminotransferase Reactionmentioning

confidence: 99%

“…The pathways for the degradation of L-arginine, D-arginine, and L-citrulline were similar to those found in A. glob~formis and B. helvolum. 8 ) However, N. simplex degraded agmatine, carbamoylputrescine, and putrescine via unique pathways.…”

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confidence: 99%

Metabolism ofL-Arginine, Agmatine, and Related Compounds inNocardioides simplex

Kaneoke

Shimizu

Yorifuji

1994

Bioscience, Biotechnology, and Biochemistry

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“…1) The arginine oxygenase pathway is distributed among Streptomyces griseus 2 ) and some bacteria related phylogenetically to actinomycetes, including Arthrobacter globiformis IFO 12137 (ATCC 8010), Brevibacterium he/volum IFO 12073, and Nocardioides simplex IFO 12069 (Arthrobacter simplex A TCC 6946). [3][4][5] On the other hand, Tochikura et al 6) have reported that N. simplex has the arginine aminotransferase pathway, which degrades Larginine to 2-ketoornithine (2-keto-5-aminovalerate) via 2-ketoarginine (2-keto-5-guanidinovalerate). Although the enzyme for the first step of the pathway was identified as arginine aminotransferase, the enzyme that hydrolyzes 2-ketoarginine to 2-ketoornithine and urea has not been identified nor characterized.…”

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confidence: 99%