Genetic diversity and expression profiles of cysteine phytases in the sheep rumen during a feeding cycle

Li, Z.; Huang, Huoqing; Zhao, Hongchang; Meng, Kun; Zhao, Jianmin; Shi, Pengjun; Yang, Peilong; Luo, Huiying; Wang, Y.; Yao, Bin

doi:10.1111/lam.12318

Cited by 5 publications

(3 citation statements)

References 14 publications

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“…In this study, while the authors performed a function-based screening of libraries generated from the whole metagenomic sequence data of forest soil to identify positive phytase activity in E. coli clones, two clones were positive for this phytase activity. Surprisingly, while phytic acid degradation activity has been restricted to only four protein superfamilies, including histidine phosphatases, tyrosine phosphatases, purple acid phosphatases, and β-propeller phosphatases [ 47 , 48 ], the two obtained proteins (MβLp01 and MβLp02) from this metagenome were annotated and identified as genes encoding for metallo-β-lactamase proteins. Sequence analysis confirmed their membership of the MβL fold superfamily of proteins due to their close protein structure homology with the MβL ZipD from E. coli , a zinc phosphodiesterase with a tRNA-processing endonuclease activity [ 49 ].…”

Section: Mβl Fold Enzymes In Bacteria: Class B β-Lactamasesmentioning

confidence: 99%

Origin, Diversity, and Multiple Roles of Enzymes with Metallo-β-Lactamase Fold from Different Organisms

Diène

Pontarotti

Azza

et al. 2023

Cells

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β-lactamase enzymes have generated significant interest due to their ability to confer resistance to the most commonly used family of antibiotics in human medicine. Among these enzymes, the class B β-lactamases are members of a superfamily of metallo-β-lactamase (MβL) fold proteins which are characterised by conserved motifs (i.e., HxHxDH) and are not only limited to bacteria. Indeed, as the result of several barriers, including low sequence similarity, default protein annotation, or untested enzymatic activity, MβL fold proteins have long been unexplored in other organisms. However, thanks to search approaches which are more sensitive compared to classical Blast analysis, such as the use of common ancestors to identify distant homologous sequences, we are now able to highlight their presence in different organisms including Bacteria, Archaea, Nanoarchaeota, Asgard, Humans, Giant viruses, and Candidate Phyla Radiation (CPR). These MβL fold proteins are multifunctional enzymes with diverse enzymatic or non-enzymatic activities of which, at least thirteen activities have been reported such as β-lactamase, ribonuclease, nuclease, glyoxalase, lactonase, phytase, ascorbic acid degradation, anti-cancer drug degradation, or membrane transport. In this review, we (i) discuss the existence of MβL fold enzymes in the different domains of life, (ii) present more suitable approaches to better investigating their homologous sequences in unsuspected sources, and (iii) report described MβL fold enzymes with demonstrated enzymatic or non-enzymatic activities.

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Section: Mβl Fold Enzymes In Bacteria: Class B β-Lactamasesmentioning

confidence: 99%

Origin, Diversity, and Multiple Roles of Enzymes with Metallo-β-Lactamase Fold from Different Organisms

Diène

Pontarotti

Azza

et al. 2023

Cells

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“…Another group of phytases comprises the relatively recently described β-propeller phosphatases (BPP-phy), which exhibit no significant homology to any known phosphatases. Furthermore, representatives of purple acid phosphatases (PAP-phy), which are mostly found in plants, and the protein tyrosine phosphatases (PTPs-phy, or cysteine phytases) that are the main phytate-degrading enzymes of ruminant animals (9), are known to exhibit phytase activity. In addition, several phytases have been associated with microbial pathogenicity in different species, i.e., a type III effector protein with phytase activity has been described as a key factor for the pathogenicity of the plant pathogen Xanthomonas .…”

Section: Introductionmentioning

confidence: 99%

Functional Metagenomics Reveals a New Catalytic Domain, the Metallo-β-Lactamase Superfamily Domain, Associated with Phytase Activity

Castillo-Villamizar

Funkner

Nacke

et al. 2019

mSphere

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Inositol-6-phosphate, also known as phytic acid, is a phosphorus source that plays several important roles in the phosphorus cycle and in cell metabolism. The known characterized enzymes responsible for its degradation, the phytases, are mostly derived from cultured individual microorganisms. The catalytic signatures of phytases are restricted to the molecular domains of four protein superfamilies: histidine phosphatases, protein tyrosine phosphatases, the purple acid phosphatases and the β-propeller phosphatases. During function-based screening of previously generated forest soil metagenomic libraries for Escherichia coli clones conferring phytase activity, two positive clones harboring the plasmids pLP05 and pLP12 were detected. Analysis of the insert sequences revealed the absence of classic phosphatase/phytase signatures of the proteins deduced from the putative genes, but the genes mblp01 (pLP05) and mblp02 (pLP12) encoded putative metallo-β-lactamases (MBLs). Several MBL representatives are promiscuous proteins with phosphoesterase activity, but phytase activity was previously not reported. Both mblp01 and mblp02 were subcloned, expressed, and analyzed. Mblp01 and Mblp02 are members of the lactamase B2 family. Protein modeling showed that the closest structural homologue of both proteins was ZipD of E. coli. Mblp01 and Mblp02 showed activity toward the majority of the tested phosphorylated substrates, including phytate. The maximal enzyme activities were recorded for Mblp01 at 50°C under acidic conditions and for Mblp02 at 35°C and a neutral pH. In the presence of Cu2+ or SDS, the activities of Mblp01 and Mblp02 were strongly inhibited. Analyses of the minimal inhibitory concentrations of several β-lactam antibiotics revealed that recombinant E. coli cells carrying mblp01 or mblp02 showed reduced sensitivity toward β-lactam antibiotics. IMPORTANCE Phytic acid is a phosphorus storage molecule in many plant tissues, a source of phosphorus alternative to phosphate rocks, but it can also be a problematic antinutrient. In comparison to other phosphorus sources, phytic acid exhibits reduced bioavailability. Additionally, it influences functions of secondary messengers and acts as antioxidant in tumor growth prevention. The enzymatic capability to process phytate has been reported for a limited number of protein families. This might be due to the almost exclusive use of proteins derived from individual microorganisms to analyze phytase activity. With such a restriction, the study of the complexity and diversity of the phytases remains incomplete. By using metagenome-derived samples, this study demonstrates the existence of phytase activity in one of the most promiscuous superfamilies, the metallo-β-lactamases. Our results increase the general knowledge on phytase diversity in environmental samples and could provide new avenues for the study and engineering of new biocatalysts.

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“…Still little is known about phytase-producing bacteria and their specific phytases, butNakashima et al (2007) found two different phytase sequences in the rumen bacterium Selenomonas lacticifex and suggested that in this bacterium multiple phytate degrading enzymes are present. Furthermore,Li et al (2014) found that phytase-producing microorganisms did not constantly secrete functional phytases, when rumen samples gained at different times after feeding were analysed. This indicates that in the rumen various phytases are available at any time leading to complete hydrolysis of InsP 6 , whereas in nonruminants, where diets are usually supplemented with only one specific phytase, lower InsPs do accumulate.Additivity of phytate degradation of compound feeds and pelleting effectCompound feeds are often pelleted, hence it is of practical value if InsP 6 ED can be calculated from that of single feeds.…”

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confidence: 99%

Determination of in situ ruminal degradation of phytate phosphorus from single and compound feeds in dairy cows using chemical analysis and near-infrared spectroscopy

Haese

Krieg

Grubješić

et al. 2020

Animal

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The ruminal degradation of P bound in phytate (InsP6) can vary between feeds, but data on ruminal degradation of InsP6 from different feedstuffs for cattle are rare. One objective of this study was to increase the data base on ruminal effective degradation of InsP6 (InsP6ED) and to assess if InsP6ED of compound feeds (CF) can be calculated from comprising single feeds. As a second objective, use of near-infrared spectroscopy (NIRS) to predict InsP6 concentrations was tested. Nine single feeds (maize, wheat, barley, faba beans, soybeans, soybean meal (SBM), rapeseed meal (RSM), sunflower meal (SFM), dried distillers’ grains with solubles (DDGS)) and two CF (CF1/CF2), consisting of different amounts of the examined single feeds, were incubated for 2, 4, 8, 16, 24, 48 and 72 h in the rumen of three ruminally fistulated Jersey cows. Samples of CF were examined before (CF1/CF2 Mash) and after pelleting (CF1/CF2 Pellet), and InsP6ED was calculated for all feeds at two passage rates (InsP6ED5: k = 5%/h; InsP6ED8: k = 8%/h). For CF1 and CF2, InsP6ED was also calculated from values of the respective single feeds. Near-infrared spectra were recorded in duplicate and used to establish calibrations to predict InsP6 concentration. Besides a global calibration, also local calibrations were evaluated by separating samples into different data sets based on their origin. The InsP6ED8 was highest for faba beans (91%), followed by maize (90%), DDGS (89%), soybeans (85%), wheat (76%) and barley (74%). Lower values were determined for oilseed meals (48% RSM, 65% SFM, 66% SBM). Calculating InsP6ED of CF from values of single feeds underestimated observed values up to 11 percentage points. The NIRS calibrations in general showed a good performance, but statistical key data suggest that local calibrations should be established. The wide variation of InsP6ED between feeds indicates that the ruminal availability of P bound in InsP6 should be evaluated individually for feeds. This requires further in situ studies with high amounts of samples for InsP6 analysis. Near-infrared spectroscopy has the potential to simplify the analytical step of InsP6 in the future, but the calibrations need to be expanded.

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Genetic diversity and expression profiles of cysteine phytases in the sheep rumen during a feeding cycle

Cited by 5 publications

References 14 publications

Origin, Diversity, and Multiple Roles of Enzymes with Metallo-β-Lactamase Fold from Different Organisms

Origin, Diversity, and Multiple Roles of Enzymes with Metallo-β-Lactamase Fold from Different Organisms

Functional Metagenomics Reveals a New Catalytic Domain, the Metallo-β-Lactamase Superfamily Domain, Associated with Phytase Activity

Determination of in situ ruminal degradation of phytate phosphorus from single and compound feeds in dairy cows using chemical analysis and near-infrared spectroscopy

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