An esterase, designated EstTs1, was identified and characterized from a genomic library of Thermus scotoductus SA-01 (ATCC 700910). The library was screened in Escherichia coli for lipolytic activity on tributyrin agar plates. A 1.7-kb DNA fragment from a lipolytic positive clone was sequenced and two open reading frames (ORFs) were identified. A 774-bp ORF, designated EstTs1 with an estimated molecular mass of 28.6 kDa, and a 693-bp ORF, designated EstTs2 with an estimated molecular mass of 25.6 kDa, were identified. These two ORFs appear to form part of an operon. Sequence analysis showed that both proteins contained the G-X-S-X-G signature sequence motif present in most esterases and lipases. The deduced amino sequence of EstTs1 was found to display significant sequence identity with putative hydrolase proteins from both Thermus aquaticus Y51MC23 and Thermus thermophilus HB27. Similarly, EstTs2, also displayed significant homology to a second putative hydrolase protein present in the same two organisms. The cloning and characterization of these two ORFs from T. aquaticus Y51MC23 and T. thermophilus strain HB27 encoding putative hydrolase genes have not been reported. E. coli cells harbouring EstTs1 on a multicopy vector produced a clearing zone on tributyrin agar plates, whereas no enzymatic activity was observed for E. coli harbouring EstTs2 on a multicopy vector. EstTs1 displayed optimum activity at pH 7 and 80 degrees C with a half life of 48 h at 70 degrees C.
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http://dx.doi.org/10.1007/s00284-009-9533-5 | DOI Listing |
PLoS One
January 2025
Department of Entomology and Plant Pathology, North Carolina State University, Raleigh, North Carolina, United States of America.
Ruvbl1 (also known as TIP49, Pontin) encodes an ATPase of the AAA+ protein superfamily involved in several cellular functions, including chromatin remodeling, control of transcription, and cellular development (motility, growth, and proliferation). While its role has been well established in model organisms including vertebrates and invertebrates (e.g.
View Article and Find Full Text PDFInt J Mol Sci
December 2024
Integrative Science Center of Germplasm Creation in Western China (CHONGQING) Science City, SWU-TAAHC Medicinal Plant Joint R&D Centre, School of Life Sciences, Southwest University, Chongqing 400715, China.
is a medicinal plant and an important source for the commercial production of tropane alkaloids (TAs), such as scopolamine and hyoscyamine, which are used clinically for their anticholinergic properties. In this study, we identified 16 metallocarboxypeptidase inhibitor (MCPI) genes from (), which are grouped into three subgroups based on phylogenetic relationships and are distributed across 10 chromosomes. Promoter analysis showed that most elements were related to defense and stress responses, such as drought, low-temperature, ABA (abscisic acid), GA (gibberellin), auxin, light and MeJA responsiveness.
View Article and Find Full Text PDFGenes (Basel)
November 2024
Jiangsu Province Key Laboratory of Animal Breeding and Molecular Design, College of Animal Science and Technology, Yangzhou University, Yangzhou 225009, China.
Background: Histone deacetylase 4 () is a member of the class II histone deacetylase family, whose members play a crucial role in various biological processes. An in-depth investigation of the transcriptional characteristics of chicken can provide fundamental insights into its function.
Methods: We examined expression in chicken embryonic stem cells (ESC) and spermatogonial stem cells (SSC) and cloned a 444 bp fragment from upstream of the chicken transcription start site.
Biomolecules
December 2024
Department of Biotechnology, Hankyong National University, Anseong 17579, Republic of Korea.
Despite the rapid advancement of glycosidase biotechnology, ginsenoside-transforming rhamnosidases remain underexplored due to a lack of research. In this study, we aimed to bridge this gap by evaluating eight putative rhamnosidases for their ability to transform ginsenosides. Among them, a novel rhamnosidase (C118) from was identified as being efficient at hydrolyzing ginsenoside Re.
View Article and Find Full Text PDFJ Biol Chem
January 2025
Department of Biology, Indian Institute of Science Education and Research, Pune, Maharashtra, India. Electronic address:
Lysophosphatidylserine (lyso-PS) is a potent hormone-like signaling lysophospholipid, which regulates many facets of mammalian biology and dysregulation in its metabolism is associated with several human neurological and autoimmune diseases. Despite the physiological importance and causal relation with human pathophysiology, little is known about the metabolism of lyso-PS in tissues other than the nervous and immune systems. To address this problem, here, we attempted to identify one (or more) lipase(s) capable of degrading lyso-PS in different mammalian tissues.
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