Purification and some properties of cyclo(Gly-Gly) hydrolase from a strain of Bacillus sp. No. 106.

Muro, Tetsuo; Tominaga, Yoshio; Okada, Shigetaka

doi:10.1271/bbb1961.49.1567

Cited by 7 publications

(4 citation statements)

References 2 publications

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“…No. 106, which was active towards one of 32 tested DKPs (Muro et al 1985 ). In contrast, a relatively wide substrate spectrum was shown for Arthrobacter sp.…”

Section: Discussionmentioning

confidence: 99%

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Enzymatical and microbial degradation of cyclic dipeptides (diketopiperazines)

2013

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Diketopiperazines (DKPs) are cyclic dipeptides, representing an abundant class of biologically active natural compounds. Despite their widespread occurrence in nature, little is known about their degradation. In this study, the enzymatical and microbial cleavage of DKPs was investigated. Peptidase catalyzed hydrolysis of certain DKPs was formerly reported, but could not be confirmed in this study. While testing additional peptidases and DKPs no degradation was detected, indicating peptidase stability of the peptide bond in cyclic dipeptides. Besides confirmation of the reported degradation of cyclo(l-Asp-l-Phe) by Paenibacillus chibensis (DSM 329) and Streptomyces flavovirens (DSM 40062), cleavage of cyclo(l-Asp-l-Asp) by DSM 329 was detected. Other DKPs were not hydrolyzed by both strains, demonstrating high substrate specificity. The degradation of cyclo(l-Asp-l-Phe) by DSM 40062 was shown to be inducible. Three strains, which are able to hydrolyze hydantoins and dihydropyrimidines, were identified for the degradation of DKPs: Leifsonia sp. K3 (DSM 27212) and Bacillus sp. A16 (DSM 25052) cleaved cyclo(dl-Ala-dl-Ala) and cyclo(l-Gly-l-Phe), and Rhizobium sp. NA04-01 (DSM 24917) degraded cyclo(l-Asp-l-Phe), cyclo(l-Gly-l-Phe) and cyclo(l-Asp-l-Asp). The first enantioselective cleavage of cyclo(dl-Ala-dl-Ala) was detected with the newly isolated strains Paenibacillus sp. 32A (DSM 27214) and Microbacterium sp. 40A (DSM 27211). Cyclo(l-Ala-d-Ala) and cyclo(l-Ala-l-Ala) were completely degraded, whereas the enantiomer cyclo(d-Ala-d-Ala) was not attacked. Altogether, five bacterial strains were newly identified for the cleavage of DKPs. These bacteria may be of value for industrial purposes, such as degradation of undesirable DKPs in food and drugs and production of (enantiopure) dipeptides and amino acids.

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“…No. 106, which was active towards one of 32 tested DKPs (Muro et al 1985 ). In contrast, a relatively wide substrate spectrum was shown for Arthrobacter sp.…”

Section: Discussionmentioning

confidence: 99%

“…Thus, it remains unclear which enzymes are responsible for the hydrolysis of DKPs. Muro et al ( 1985 ) concluded, that the cyclo(Gly-Gly) hydrolase of Bacillus sp. No.…”

Section: Discussionmentioning

confidence: 99%

Enzymatical and microbial degradation of cyclic dipeptides (diketopiperazines)

2013

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“…No. 106 but only catalyzed the hydrolysis of cyclo(Gly-Gly) among a variety of 2,5-DKPs tested . In contrast the 2,5-DKP-hydrolyzing enzymes produced intracellularly by Arthrobacter sp.…”

Section: Reactionsmentioning

confidence: 96%

“…2,5-DKP-hydrolyzing enzymes are produced by a range of bacteria. − Cyclo(Gly-Gly) hydrolase is secreted from Bacillus sp. No.…”

Section: Reactionsmentioning

confidence: 99%

2,5-Diketopiperazines: Synthesis, Reactions, Medicinal Chemistry, and Bioactive Natural Products

Borthwick¹

2012

Chem. Rev.

741

726

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amide with a bivalent electrophile. For example, the aminoamide adducts 118 of tryptamine and an L-amino acid were reacted with a range of pyruvic acids to give the ketoamides 119. These were cyclized with HCl in EtOAc to give the 2,5-DKP ring that underwent a Pictet−Spengler-type condensation to give the tetrahydro-β-carboline and tetrahydroisoquinoline 2,5-diketopiperazines 120a and 120b. 102 However, reacting 118 (R = 5,6-DiMeO, R 1 = Me) with pyruvic acid gave the hydroxylactam 121 as a mixture of diastereroisomers rather than the ketoamide, and they underwent cyclization in the presence of HCl to give the corresponding tetrahydroisoquinoline 2,5-diketopiperazine derivatives 120b (Scheme 30). The L-amino acids were promoters of 1,4-chirality transfer with up to 100% diastereomeric excess (de). The stereochemistry of the final 2,5-diketopiperazines strongly depended on the structure of the L-amino acids used: acyclic amino acids gave predominantly the (R)-configuration at the newly created stereogenic center, whereas L-proline afforded the opposite configuration 122.

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2,5-Dioxopiperazine hydrolase

Schomburg

Stephan

1998

Enzyme Handbook 16

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Purification and some properties of cyclo(Gly-Gly) hydrolase from a strain of Bacillus sp. No. 106.

Cited by 7 publications

References 2 publications

Enzymatical and microbial degradation of cyclic dipeptides (diketopiperazines)

Enzymatical and microbial degradation of cyclic dipeptides (diketopiperazines)

2,5-Diketopiperazines: Synthesis, Reactions, Medicinal Chemistry, and Bioactive Natural Products

2,5-Dioxopiperazine hydrolase

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