Cyclic-Imide-Hydrolyzing Activity of
            <scp>d</scp>
            -Hydantoinase from
            <i>Blastobacter</i>
            sp. Strain A17p-4

Soong, Chee-Leong; Ogawa, Jun; Honda, Michinari; Shimizu, Sakayu

doi:10.1128/aem.65.4.1459-1462.1999

Cited by 31 publications

(5 citation statements)

References 24 publications

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“…The substrate specificities and biological function of these enzymes vary widely, including carbon/nitrogen metabolism in fungi through the hydrolysis of acetamide , generation of properly charged tRNA Gln in eubacteria through glutamine , and the degradation of neuromodulatory fatty acids . Fatty acid amide hydrolase (FAAH) belongs to a large class of hydrolytic enzymes termed the Amidase Signature Family whose members have a conserved sketch of approximately 130 amino acids termed the AS sequence .…”

Section: Nitrilase Superfamilymentioning

confidence: 99%

Nitrile‐converting enzymes: An eco‐friendly tool for industrial biocatalysis

Ramteke

Maurice

Joseph

et al. 2013

Biotech and App Biochem

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Nitriles are organic compounds bearing a − C ≡ N group; they are frequently known to occur naturally in both fauna and flora and are also synthesized chemically. They have wide applicability in the fields of medicine, industry, and environmental monitoring. However, the majority of nitrile compounds are considered to be lethal, mutagenic, and carcinogenic in nature and are known to cause potential health problems such as nausea, bronchial irritation, respiratory distress, convulsions, coma, and skeletal deformities in humans. Nitrile-converting enzymes, which are extracted from microorganisms, are commonly termed nitrilases and have drawn the attention of researchers all over the world to combat the toxicity of nitrile compounds. The present review focuses on the utility of nitrile-converting enzymes, sources, classification, structure, properties, and applications, as well as the future perspective on nitrilases.

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Section: Nitrilase Superfamilymentioning

confidence: 99%

Nitrile‐converting enzymes: An eco‐friendly tool for industrial biocatalysis

Ramteke

Maurice

Joseph

et al. 2013

Biotech and App Biochem

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“…Moreover, it was noted the forming of singular resistant colonies of some strains of P. uorescence, after few days of cultivation on nutrient agar cultural media. Probably, this effect is being de ned by selection of resistant mutants and is related with some enzymatic activity, for example polyphenol oxidases activity of Pseudomonas [Bagdasaryan et al 2019;Janusz et al 2020;Soong et al 1999].…”

Section: Strainmentioning

confidence: 99%

Tartaric Acid Synthetic Derivatives Activity Against Pseudomonas, Strenotrophomonas, Xanthomonas Phytopathogens and Oppotunistic Pathogens

Grigoryan¹,

Baghdasaryan²,

Babayan³

et al. 2021

Preprint

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The multi-drug resistance is one of the most actual medical and ecological problem. Stenotrophomonas, Xanthomonas, Pseudomonas are common, drug resistant and highly adaptive phytopathogenic and opportunistic pathogenic microbes. Tartaric acid is natural safe antimicrobial agent. In current paper it is discussed the synthesis and antimicrobial activity of tartaric acid new derivatives, which were investigated in our laboratory. There were obtained benzyl, cyclohexyl and phenyl substituted imides as well as complex amine salts of tartaric acid. Their antimicrobial activity was tested on native soil Pseudomonas, Xanthomonas and Stenotrophomonas different strains from The National Microbe Collection of Scientific and Production Center (SPC) “Armbiotechnology” National Academy of Sciences of Republic of Armenia (NAS RA).As a result of cultivation on appropriate compound containing media, as well as genetical analyses of tested microbes and docking analyses, it was found out that tartaric acid carbocyclic and aromatic imides and complex salts are effective as non-selective growth inhibitors. Complex salts of tartaric acid are biodegradable by some soil strains of P. chlororaphis, etc. Thus, all the elaborated compounds can be recommended for further study of their activity as an effective alternative against the multi-drug resistant microorganisms.

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“…ALLase [ 14 ] is a member of the cyclic amidohydrolase family [ 15 , 16 ], which also includes dihydroorotase (DHOase) [ 17 , 18 , 19 , 20 , 21 , 22 , 23 ], dihydropyrimidinase (DHPase) [ 24 , 25 , 26 , 27 , 28 , 29 , 30 , 31 ], hydantoinase (HYDase) [ 32 , 33 , 34 ], and imidase [ 35 , 36 , 37 ]. Almost all these enzymes contain the binuclear metal center that consists of four His, one Asp, and one posttranslational carbamylated Lys (Kcx) residues [ 15 ].…”

Section: Introductionmentioning

confidence: 99%

Crystal Structure of Allantoinase from Escherichia coli BL21: A Molecular Insight into a Role of the Active Site Loops in Catalysis

et al. 2023

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Allantoinase (ALLase; EC 3.5.2.5) possesses a binuclear metal center in which two metal ions are bridged by a posttranslationally carbamylated lysine. ALLase acts as a key enzyme for the biogenesis and degradation of ureides by catalyzing the conversion of allantoin into allantoate. Biochemically, ALLase belongs to the cyclic amidohydrolase family, which also includes dihydropyrimidinase, dihydroorotase, hydantoinase (HYDase), and imidase. Previously, the crystal structure of ALLase from Escherichia coli K-12 (EcALLase-K12) was reported; however, the two active site loops crucial for substrate binding were not determined. This situation would limit further docking and protein engineering experiments. Here, we solved the crystal structure of E. coli BL21 ALLase (EcALLase-BL21) at a resolution of 2.07 Å (PDB ID 8HFD) to obtain more information for structural analyses. The structure has a classic TIM barrel fold. As compared with the previous work, the two missed active site loops in EcALLase-K12 were clearly determined in our structure of EcALLase-BL21. EcALLase-BL21 shared active site similarity with HYDase, an important biocatalyst for industrial production of semisynthetic penicillin and cephalosporins. Based on this structural comparison, we discussed the functional role of the two active site loops in EcALLase-BL21 to better understand the substrate/inhibitor binding mechanism for further biotechnological and pharmaceutical applications.

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Cyclic-Imide-Hydrolyzing Activity of d -Hydantoinase from Blastobacter sp. Strain A17p-4

Cited by 31 publications

References 24 publications

Nitrile‐converting enzymes: An eco‐friendly tool for industrial biocatalysis

Nitrile‐converting enzymes: An eco‐friendly tool for industrial biocatalysis

Tartaric Acid Synthetic Derivatives Activity Against Pseudomonas, Strenotrophomonas, Xanthomonas Phytopathogens and Oppotunistic Pathogens

Crystal Structure of Allantoinase from Escherichia coli BL21: A Molecular Insight into a Role of the Active Site Loops in Catalysis

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