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AmiP from hyperther...
AmiP from hyperthermophilic Thermus parvatiensis prophage is a thermoactive and ultrathermostable peptidoglycan lytic amidase
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- Jasilionis, Andrius (författare)
- Lund University,Lunds universitet,Bioteknik,Centrum för tillämpade biovetenskaper,Kemiska institutionen,Institutioner vid LTH,Lunds Tekniska Högskola,Biotechnology,Center for Applied Life Sciences,Department of Chemistry,Departments at LTH,Faculty of Engineering, LTH
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- Plotka, Magdalena (författare)
- University of Gdansk
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- Wang, Lei (författare)
- University of Stuttgart
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visa fler...
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- Dorawa, Sebastian (författare)
- University of Gdansk
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- Lange, Joanna (författare)
- Bio-prodict BV
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- Watzlawick, Hildegard (författare)
- University of Stuttgart
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- van den Bergh, Tom (författare)
- Bio-prodict BV
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- Vroling, Bas (författare)
- Bio-prodict BV
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- Altenbuchner, Josef (författare)
- University of Stuttgart
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- Kaczorowska, Anna-Karina (författare)
- University of Gdansk
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- Pohl, Ehmke (författare)
- Durham University
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- Kaczorowski, Tadeusz (författare)
- University of Gdansk
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- Nordberg Karlsson, Eva (författare)
- Lund University,Lunds universitet,Bioteknik,Centrum för tillämpade biovetenskaper,Kemiska institutionen,Institutioner vid LTH,Lunds Tekniska Högskola,Biotechnology,Center for Applied Life Sciences,Department of Chemistry,Departments at LTH,Faculty of Engineering, LTH
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- Freitag-Pohl, Stefanie (författare)
- Durham University
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visa färre...
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(creator_code:org_t)
- 2023-02-15
- 2023
- Engelska 19 s.
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Ingår i: Protein Science. - : Wiley. - 1469-896X .- 0961-8368. ; 32:3, s. 4585-4585
- Relaterad länk:
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http://dx.doi.org/10... (free)
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https://lup.lub.lu.s...
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https://doi.org/10.1...
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Abstract
Ämnesord
Stäng
- Bacteriophages encode a wide variety of cell wall disrupting enzymes that aid the viral escape in the final stages of infection. These lytic enzymes have accumulated notable interest due to their potential as novel antibacterials for infection treatment caused by multiple-drug resistant bacteria. Here, the detailed functional and structural characterization of Thermus parvatiensis prophage peptidoglycan lytic amidase AmiP, a globular Amidase_3 type lytic enzyme adapted to high temperatures is presented. The sequence and structure comparison with homologous lytic amidases reveals the key adaptation traits that ensure the activity and stability of AmiP at high temperatures. The crystal structure determined at a resolution of 1.8 Å displays a compact α/β-fold with multiple secondary structure elements omitted or shortened compared with protein structures of similar proteins. The functional characterization of AmiP demonstrates high efficiency of catalytic activity and broad substrate specificity toward thermophilic and mesophilic bacteria strains containing Orn-type or DAP-type peptidoglycan. The here presented AmiP constitutes the most thermoactive and ultrathermostable Amidase_3 type lytic enzyme biochemically characterized with a temperature optimum at 85°C. The extraordinary high melting temperature Tm 102.6°C confirms fold stability up to approximately 100°C. Furthermore, AmiP is shown to be more active over the alkaline pH range with pH optimum at pH 8.5 and tolerates NaCl up to 300 mM with the activity optimum at 25 mM NaCl. This set of beneficial characteristics suggests that AmiP can be further exploited in biotechnology.
Ämnesord
- NATURVETENSKAP -- Biologi -- Biokemi och molekylärbiologi (hsv//swe)
- NATURAL SCIENCES -- Biological Sciences -- Biochemistry and Molecular Biology (hsv//eng)
Nyckelord
- adaptation
- Amidase_3 catalytic domain
- peptidoglycan lytic amidases
- thermoactivity
- thermostability
- Thermus prophage
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Jasilionis, Andr ...
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Plotka, Magdalen ...
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Wang, Lei
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Dorawa, Sebastia ...
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Lange, Joanna
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Watzlawick, Hild ...
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visa fler...
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van den Bergh, T ...
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Vroling, Bas
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Altenbuchner, Jo ...
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Kaczorowska, Ann ...
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Pohl, Ehmke
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Kaczorowski, Tad ...
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Nordberg Karlsso ...
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Freitag-Pohl, St ...
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visa färre...
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- NATURVETENSKAP
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NATURVETENSKAP
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och Biologi
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och Biokemi och mole ...
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Protein Science
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Lunds universitet