The SGNH-hydrolase of Streptomyces coelicolor has (aryl)esterase and a true lipase activity

Bielen, Ana; Ćetković, Helena; Long, Paul F.; Schwab, Helmut; Abramić, Marija; Vujaklija, Dušica

doi:10.1016/j.biochi.2008.10.018

Cited by 40 publications

(43 citation statements)

References 47 publications

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“…These proteins are probably involved in degradation of extracellular or capsular material, facilitating phage infection. SGNH proteins are involved in the hydrolysis of a wide variety of substrates, including fatty acids, aromatic esters, and amino acid derivatives [37]. Pectin lyase proteins have been described as putative hydrolases against extracellular components from bacterial biofilms [38].…”

Section: Discussionmentioning

confidence: 99%

Three proposed new bacteriophage genera of staphylococcal phages: “3alikevirus”, “77likevirus” and “Phietalikevirus”

et al. 2013

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Section: Discussionmentioning

confidence: 99%

Three proposed new bacteriophage genera of staphylococcal phages: “3alikevirus”, “77likevirus” and “Phietalikevirus”

et al. 2013

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“…Less commonly, recombinant lipases have also been expressed in the yeast, Saccharomyces cerevisiae (Florczak et al 2013), and the fungi, Streptomyces sp. (Bielen et al 2009) and Trichoderma sp. (Qin et al 2012).…”

Section: Molecular Studiesmentioning

confidence: 99%

An insight into microbial lipases and their environmental facet

Kanmani¹,

Aravind²,

Kumaresan³

2014

Int. J. Environ. Sci. Technol.

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Lipases are serine hydrolases that catalyze the hydrolysis and synthesis of esters formed from glycerol and long-chain fatty acids, by acting at the oil-water interface. Lipases from microbial sources have received heightened attention for an array of industrial applications, and these enzymes have been well exploited in the environmental sector as well. In this article, we present an overview of microbial lipase, including the microorganisms from which it could be produced; the application of recombinant DNA technology tools to produce lipase with enhanced properties, the effective use of waste materials as substrates for lipase production; the usage of statistical tools to efficiently optimize the production medium; lipase purification strategies; and the immobilization of the enzyme on a variety of support materials. The next section of the article provides a gist of its application in diversified spheres and focusses exclusively on the environmentally relevant ones. Lipasecatalyzed esterification, transesterification, and interesterification reactions, an emerging area of green chemistry; lipase-mediated in vitro biopolymer synthesis and degradation; and the application of lipase for remediating fat and oil constituents in wastewater are dealt with in-depth. When its full potential is harnessed, the enzyme could play a pivotal role in environmental management.

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“…GDSL/SGNH hydrolase domain proteins are involved in the hydrolysis of wide variety of substrates, including fatty acids, aromatic esters, and amino acid derivatives, and are particularly abundant in Actinomycetes (3,6). These relationships suggested that this gene clusters might encode proteins that interact with the cell envelope in Rhodococcus.…”

Section: Vol 77 2011 Genomic and Functional Analyses Of R Equi Phamentioning

confidence: 99%

Genomic and Functional Analyses of Rhodococcus equi Phages ReqiPepy6, ReqiPoco6, ReqiPine5, and ReqiDocB7

Summer

Liu

Gill

et al. 2011

Appl Environ Microbiol

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The isolation and results of genomic and functional analyses of Rhodococcus equi phages ReqiPepy6, ReqiDocB7, ReqiPine5, and ReqiPoco6 (hereafter referred to as Pepy6, DocB7, Pine5, and Poco6, respectively) are reported. Two phages, Pepy6 and Poco6, more than 75% identical, exhibited genome organization and protein sequence likeness to Lactococcus lactis phage 1706 and clostridial prophage elements. An unusually high fraction, 27%, of Pepy6 and Poco6 proteins were predicted to possess at least one transmembrane domain, a value much higher than the average of 8.5% transmembrane domain-containing proteins determined from a data set of 36,324 phage protein entries. Genome organization and protein sequence comparisons place phage Pine5 as the first nonmycobacteriophage member of the large Rosebush cluster. DocB7, which had the broadest host range among the four isolates, was not closely related to any phage or prophage in the database, and only 23 of 105 predicted encoded proteins could be assigned a functional annotation. Because of the relationship of Rhodococcus to Mycobacterium, it was anticipated that these phages should exhibit some of the features characteristic of mycobacteriophages. Traits that were identified as shared by the Rhodococcus phages and mycobacteriophages include the prevalent long-tailed morphology and the presence of genes encoding LysBlike mycolate-hydrolyzing lysis proteins. Application of DocB7 lysates to soils amended with a host strain of R. equi reduced recoverable bacterial CFU, suggesting that phage may be useful in limiting R. equi load in the environment while foals are susceptible to infection.Although the "tailed phage," or members of the virus order Caudovirales, constitute the majority of DNA diversity on the planet, the genomes of only a few hundred are known. Moreover, the genomic data that are available for bacteriophages are extremely unevenly distributed in terms of host species, with two-thirds derived from phages of only eight host genera or closely related bacterial species, including those belonging to the Staphylococcus, Mycobacterium, Pseudomonas, Lactococcus, and Burkholderia genera and the Enterobacteriaceae family (28). Nevertheless, some important themes have emerged from analyzing multiple phages that infect closely related host genera. One theme emerging is that despite rampant lateral gene transfer, there are recognizable "phage types" spanning geography and host taxa. Casjens (11a) was able to group 73 tailed-enterophage genomes into 13 phage types, the members of which were more closely related to each other by a number of criteria than they were to any member of another type. It should be noted that the classic enterophages do not include representatives of all phage types. When groups of phages from other host clades are sequenced, new phages and new phage types are identified. For example, among the sequenced phages of Burkholderia, there are members of the established , Mu, and P2 temperate phage types, as well as entirely new virulent phage types, such a...

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The SGNH-hydrolase of Streptomyces coelicolor has (aryl)esterase and a true lipase activity

Cited by 40 publications

References 47 publications

Three proposed new bacteriophage genera of staphylococcal phages: “3alikevirus”, “77likevirus” and “Phietalikevirus”

Three proposed new bacteriophage genera of staphylococcal phages: “3alikevirus”, “77likevirus” and “Phietalikevirus”

An insight into microbial lipases and their environmental facet

Genomic and Functional Analyses of Rhodococcus equi Phages ReqiPepy6, ReqiPoco6, ReqiPine5, and ReqiDocB7

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