Amidases: versatile enzymes in nature

Sharma, Monica; Sharma, Nitya; Bhalla, Tek Chand

doi:10.1007/s11157-009-9175-x

Cited by 81 publications

(39 citation statements)

References 128 publications

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“…It can be catalyzed by amidases and proteolytic enzymes [46,47]. While these enzymes were not found in Nitrosomonas eutropaea [48], two genes found in Nitrosomonas eutropha including Nacetylmuramoyl-L-alanine amidase (Neut_1623) and amidohydrolase-2 (Neut_1622) could favor the hydrolysis of the C-N bond of amide groups [49].…”

Section: Biodegradation Pathways By Enriched Nitrifying Sludgementioning

confidence: 99%

Biodegradation of atenolol by an enriched nitrifying sludge: Products and pathways

Radjenović

Yuan

et al. 2017

Chemical Engineering Journal

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Biodegradation of β-blocker atenolol was investigated using an enriched nitrifying culture at controlled ammonium concentration and without ammonium addition. Analysis of the kinetics and structural elucidation of biodegradation products showed that atenolol biodegradation was found to be linked to the activity of nitrifying bacteria in the presence of ammonium. Atenolol was degraded cometabolically by ammonia-oxidizing bacteria (AOB), likely due to a broad substrate range of ammonia monooxyenase (AMO). Four products were formed during atenolol biodegradation with ammonia oxidation, including P267 (atenolol acid) and three new products P117 (1-isopropylamino-2-propanol), P167 (1-amino-3-phenoxy-2-propanol), and an unknown product P227 with a nominal molecular mass of 227. In comparison, only P267 and P227 were identified during atenolol biodegradation without ammonia oxidation. Follow-up experiments using atenolol acid as the parent compound indicated the formation of products P117, P167 and P227 in the presence of ammonium. Based on the products identified, a tentative biodegradation pathway of atenolol is suggested, which involves two steps independent of the presence of ammonium: i) microbial amide-bond hydrolysis to carboxyl group and formation of P267 (atenolol acid) and ii) a possible formation of P227 with its unidentified structure and other two cometabolically induced reactions: iii) breakage of ether bond in the alkyl side chain and formation of P117 and iv) a minor pathway through N-dealkylation and loss of acetamide moiety from the aromatic ring, yielding P167. This study provided an important insight regarding the biotransformation pathways under different metabolic conditions.

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Section: Biodegradation Pathways By Enriched Nitrifying Sludgementioning

confidence: 99%

Biodegradation of atenolol by an enriched nitrifying sludge: Products and pathways

Radjenović

Yuan

et al. 2017

Chemical Engineering Journal

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“…Current understanding of their functions is limited (51) because speculating about them from sequence information is difficult. The present report is the first to provide information about the amino acid sequence of hydrazidase and will contribute to future studies on the distribution of hydrazidases and their sources in nature.…”

Section: Discussionmentioning

confidence: 99%

Hydrazidase, a Novel Amidase Signature Enzyme That Hydrolyzes Acylhydrazides

et al. 2015

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The degradation mechanisms of natural and artificial hydrazides have been elucidated. Here we screened and isolated bacteria that utilize the acylhydrazide 4-hydroxybenzoic acid 1-phenylethylidene hydrazide (HBPH) from soils. Physiological and phylogenetic studies identified one bacterium as Microbacterium sp. strain HM58-2, from which we purified intracellular hydrazidase, cloned its gene, and prepared recombinant hydrazidase using an Escherichia coli expression system. The Microbacterium sp. HM58-2 hydrazidase is a 631-amino-acid monomer that was 31% identical to indoleacetamide hydrolase isolated from Bradyrhizobium japonicum. Phylogenetic studies indicated that the Microbacterium sp. HM58-2 hydrazidase constitutes a novel hydrazidase group among amidase signature proteins that are distributed within proteobacteria, actinobacteria, and firmicutes. The hydrazidase stoichiometrically hydrolyzed the acylhydrazide residue of HBPH to the corresponding acid and hydrazine derivative. Steady-state kinetics showed that the enzyme hydrolyzes structurally related 4-hydrozybenzamide to hydroxybenzoic acid at a lower rate than HBPH, indicating that the hydrazidase prefers hydrazide to amide. The hydrazidase contains the catalytic Ser-Ser-Lys motif that is conserved among members of the amidase signature family; it shares a catalytic mechanism with amidases, according to mutagenesis findings, and another hydrazidase-specific mechanism must exist that compensates for the absence of the catalytic Ser residue. The finding that an environmental bacterium produces hydrazidase implies the existence of a novel bacterial mechanism of hydrazide degradation that impacts its ecological role.

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“…Since last few years, amidases emerged as a versatile biocatalyst in white and green chemistry. They are widely investigated by researchers due to their enantio/stereoselective properties (Sharma et al 2009). …”

Section: Introductionmentioning

confidence: 99%

Production optimization of extracellular amidase enzyme by newly isolated Pseudomonas putida AP-2 from agricultural soil

Abada

2014

Rend. Fis. Acc. Lincei

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Amidases are ubiquitous enzymes that have received increased attention due to their wide range of biotechnological applications, especially in industries for the synthesis of wide variety of carboxylic and hydroxamic acids, which find applications in pharmaceuticals, agrochemicals and waste water treatments. In the present study, 40 bacterial isolates were screened for extracellular amidase-producing capability, and on the basis of color development, 5 isolates were selected for amidase production in broth media. Based on enzyme production, one of the most potent isolates identified as Pseudomonas putida AP-2 was selected for further study. The effects of media composition and various fermentation conditions for optimization of amidase production were studied. The maximum extracellular amidase production was obtained at 30°C and pH 8.0 after 36 h of incubation in shaking condition. Among the substrate, acetamide was the best; however, P. putida AP-2 also utilized acrylamide which is a known carcinogen. Regarding carbon sources, glucose was the best, while peptone was found the best nitrogen source. The isolated bacterium, P. putida AP-2, is also tolerant to number of heavy metals at higher levels so this may also be applied for field application in contaminated soil.

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Amidases: versatile enzymes in nature

Cited by 81 publications

References 128 publications

Biodegradation of atenolol by an enriched nitrifying sludge: Products and pathways

Biodegradation of atenolol by an enriched nitrifying sludge: Products and pathways

Hydrazidase, a Novel Amidase Signature Enzyme That Hydrolyzes Acylhydrazides

Production optimization of extracellular amidase enzyme by newly isolated Pseudomonas putida AP-2 from agricultural soil

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