The C-Type Lysozyme from the upper Gastrointestinal Tract of Opisthocomus hoatzin, the Stinkbird

Taylor, Edward J.; Skjøt, Michael; Skov, L.K.; Klausen, Mikkel; Maria, Leonardo De; Gippert, Garry P.; Turkenburg, J.P.; Davies, G.J.; Wilson, K.S.

doi:10.3390/ijms20225531

Cited by 7 publications

(5 citation statements)

References 34 publications

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“…The optimum is at pH 4.0, but the activity profiles are quite broad, especially for Aa Mur. This is in the same range as for GH22 lysozymes from ruminants [ 33 ] and the stinkbird [ 13 ], while HEWL has its optimum at higher pH (6–7). However, the peptidoglycan molecule is a charged substrate with its own pI and since peptidoglycan varies dependent on species the resulting pH optimum will vary.…”

Section: Resultssupporting

confidence: 55%

“…Our aim was to identify a different type of muramidase to act as a feed additive for processing bacterial debris in the gut of animals (particularly chickens). For this application gastric stability is an important property that limits the use of HEWL as a feed additive [ 13 ]. We further required that the enzyme is not toxic to the usual set of bacterial flora—i.e.…”

Section: Introductionmentioning

confidence: 99%

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Fungal GH25 muramidases: New family members with applications in animal nutrition and a crystal structure at 0.78Å resolution

et al. 2021

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Muramidases/lysozymes hydrolyse the peptidoglycan component of the bacterial cell wall. They are found in many of the glycoside hydrolase (GH) families. Family GH25 contains muramidases/lysozymes, known as CH type lysozymes, as they were initially discovered in the Chalaropsis species of fungus. The characterized enzymes from GH25 exhibit both β-1,4-N-acetyl- and β-1,4-N,6-O-diacetylmuramidase activities, cleaving the β-1,4-glycosidic bond between N-acetylmuramic acid (NAM) and N-acetylglucosamine (NAG) moieties in the carbohydrate backbone of bacterial peptidoglycan. Here, a set of fungal GH25 muramidases were identified from a sequence search, cloned and expressed and screened for their ability to digest bacterial peptidoglycan, to be used in a commercial application in chicken feed. The screen identified the enzyme from Acremonium alcalophilum JCM 736 as a suitable candidate for this purpose and its relevant biochemical and biophysical and properties are described. We report the crystal structure of the A. alcalophilum enzyme at atomic, 0.78 Å resolution, together with that of its homologue from Trichobolus zukalii at 1.4 Å, and compare these with the structures of homologues. GH25 enzymes offer a new solution in animal feed applications such as for processing bacterial debris in the animal gut.

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Section: Resultssupporting

confidence: 55%

Section: Introductionmentioning

confidence: 99%

Fungal GH25 muramidases: New family members with applications in animal nutrition and a crystal structure at 0.78Å resolution

et al. 2021

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“…3.1. A fungal GH24 muramidase with a CWBD from T. saccata A broad bioinformatic screening for new muramidases from known GH families (GH22-GH25; Taylor et al, 2019;Moroz et al, 2021) led to the discovery of an enzyme from T. saccata with an extra domain attached to the catalytic GH24 domain. As described below, we demonstrate that this is an SH3-like cell-wall-binding domain (CWBD).…”

Section: Resultsmentioning

confidence: 99%

Module walking using an SH3-like cell-wall-binding domain leads to a new GH184 family of muramidases

Moroz

Blagova

Лебедев

et al. 2023

Acta Cryst Sect D Struct Biol

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Muramidases (also known as lysozymes) hydrolyse the peptidoglycan component of the bacterial cell wall and are found in many glycoside hydrolase (GH) families. Similar to other glycoside hydrolases, muramidases sometimes have noncatalytic domains that facilitate their interaction with the substrate. Here, the identification, characterization and X-ray structure of a novel fungal GH24 muramidase from Trichophaea saccata is first described, in which an SH3-like cell-wall-binding domain (CWBD) was identified by structure comparison in addition to its catalytic domain. Further, a complex between a triglycine peptide and the CWBD from T. saccata is presented that shows a possible anchor point of the peptidoglycan on the CWBD. A `domain-walking' approach, searching for other sequences with a domain of unknown function appended to the CWBD, was then used to identify a group of fungal muramidases that also contain homologous SH3-like cell-wall-binding modules, the catalytic domains of which define a new GH family. The properties of some representative members of this family are described as well as X-ray structures of the independent catalytic and SH3-like domains of the Kionochaeta sp., Thermothielavioides terrestris and Penicillium virgatum enzymes. This work confirms the power of the module-walking approach, extends the library of known GH families and adds a new noncatalytic module to the muramidase arsenal.

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“…The main principle in DNA extraction is lysis and extraction of tissue of bacterial wall and its components which then purified to to obtain a high quality and purity of DNA sample. [8] The results of DNA isolates were tested quantitatively using the GE Nanovue UV-Vis Spectrophotometer shown in the Table. 1 below.…”

Section: Isolation and Characterizationmentioning

confidence: 99%

Primer concentration and Pre-denaturation Time Effect on cyt-K Bacillus cereus Detection using Real-Time PCR Method

Azzahra,

Nurjayadi,

Pramudiyasih

et al. 2023

E3S Web Conf.

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Foodborne disease is a global threat that can affect all sections of society, both in developed or developing countries. Bacillus cereus is a Gram-positive bacteria that can cause food poisoning disease in humans. [2] Real-Time PCR detection method is one of the molecular marker methods that has been widely recognized as a fast, reliable, sensitive and specific detection tool for detecting pathogenic bacteria. In previous studies, the optimum condition and formulas applied for cyt-K 2 primer pairs have been obtained using Real-Time PCR. The purpose of this study is to find out the best conditions work of the primer pair cyt-K Bacillus cereus on detecting bacteria target using variations of pre-denaturation time and primer concentration with Real-Time PCR method. The annealing temperature used for PCR is at 60°C with sample concentration 50 ng/µL of B. cereus. Real-time PCR detection of variations in pre-denaturation time and primer concentration obtained the best conditions for primer pair cyt-K work at minute 4 with a primer concentration of 10 pmol and successfully amplifying the target by producing a Ct value of B. cereus at 13.04. Based on the results of the study, the primer pair cyt-K were reproducible in detecting the target gene and in the further step, this research can be continued to developed a prototype detection kit for foodborne pathogen bacteria using Real-Time PCR method.

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The C-Type Lysozyme from the upper Gastrointestinal Tract of Opisthocomus hoatzin, the Stinkbird

Cited by 7 publications

References 34 publications

Fungal GH25 muramidases: New family members with applications in animal nutrition and a crystal structure at 0.78Å resolution

Fungal GH25 muramidases: New family members with applications in animal nutrition and a crystal structure at 0.78Å resolution

Module walking using an SH3-like cell-wall-binding domain leads to a new GH184 family of muramidases

Primer concentration and Pre-denaturation Time Effect on cyt-K Bacillus cereus Detection using Real-Time PCR Method

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