AmiP from hyperthermophilic Thermus parvatiensis prophage is a thermoactive and ultrathermostable peptidoglycan lytic amidase
(2023) In Protein Science 32(3). p.4585-4585- Abstract
- 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... (More) - 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. (Less)
Please use this url to cite or link to this publication:
https://lup.lub.lu.se/record/661b34d7-d02c-4d61-b125-4c3b96e2a776
- author
- Jasilionis, Andrius
LU
; Plotka, Magdalena
; Wang, Lei
; Dorawa, Sebastian
; Lange, Joanna
; Watzlawick, Hildegard
; van den Bergh, Tom
; Vroling, Bas
; Altenbuchner, Josef
; Kaczorowska, Anna-Karina
; Pohl, Ehmke
; Kaczorowski, Tadeusz
; Nordberg Karlsson, Eva
LU
and Freitag-Pohl, Stefanie
(Less) - organization
- publishing date
- 2023
- type
- Contribution to journal
- publication status
- published
- subject
- keywords
- adaptation, Amidase_3 catalytic domain, peptidoglycan lytic amidases, thermoactivity, thermostability, Thermus prophage
- in
- Protein Science
- volume
- 32
- issue
- 3
- pages
- 19 pages
- publisher
- The Protein Society
- external identifiers
-
- pmid:36721347
- scopus:85148965910
- ISSN
- 1469-896X
- DOI
- 10.1002/pro.4585
- language
- English
- LU publication?
- yes
- additional info
- This article is protected by copyright. All rights reserved.
- id
- 661b34d7-d02c-4d61-b125-4c3b96e2a776
- date added to LUP
- 2023-02-16 13:40:25
- date last changed
- 2024-06-12 08:18:50
@article{661b34d7-d02c-4d61-b125-4c3b96e2a776,
abstract = {{Bacteriophages encode a wide variety of cell wall disrupting enzymes <br>
that aid the viral escape in the final stages of infection. These lytic <br>
enzymes have accumulated notable interest due to their potential as <br>
novel antibacterials for infection treatment caused by multiple-drug <br>
resistant bacteria. Here, the detailed functional and structural <br>
characterization of <i>Thermus parvatiensis</i> prophage peptidoglycan <br>
lytic amidase AmiP, a globular Amidase_3 type lytic enzyme adapted to <br>
high temperatures is presented. The sequence and structure comparison <br>
with homologous lytic amidases reveals the key adaptation traits that <br>
ensure the activity and stability of AmiP at high temperatures. The <br>
crystal structure determined at a resolution of 1.8 Å displays a compact<br>
α/β-fold with multiple secondary structure elements omitted or <br>
shortened compared with protein structures of similar proteins. The <br>
functional characterization of AmiP demonstrates high efficiency of <br>
catalytic activity and broad substrate specificity toward thermophilic <br>
and mesophilic bacteria strains containing Orn-type or DAP-type <br>
peptidoglycan. The here presented AmiP constitutes the most thermoactive<br>
and ultrathermostable Amidase_3 type lytic enzyme biochemically <br>
characterized with a temperature optimum at 85°C. The extraordinary high<br>
melting temperature <i>T</i><sub>m</sub> 102.6°C confirms fold <br>
stability up to approximately 100°C. Furthermore, AmiP is shown to be <br>
more active over the alkaline pH range with pH optimum at pH 8.5 and <br>
tolerates NaCl up to 300 mM with the activity optimum at 25 mM NaCl. <br>
This set of beneficial characteristics suggests that AmiP can be further<br>
exploited in biotechnology.}},
author = {{Jasilionis, Andrius and Plotka, Magdalena and Wang, Lei and Dorawa, Sebastian and Lange, Joanna and Watzlawick, Hildegard and van den Bergh, Tom and Vroling, Bas and Altenbuchner, Josef and Kaczorowska, Anna-Karina and Pohl, Ehmke and Kaczorowski, Tadeusz and Nordberg Karlsson, Eva and Freitag-Pohl, Stefanie}},
issn = {{1469-896X}},
keywords = {{adaptation; Amidase_3 catalytic domain; peptidoglycan lytic amidases; thermoactivity; thermostability; Thermus prophage}},
language = {{eng}},
number = {{3}},
pages = {{4585--4585}},
publisher = {{The Protein Society}},
series = {{Protein Science}},
title = {{AmiP from hyperthermophilic <i>Thermus parvatiensis</i> prophage is a thermoactive and ultrathermostable peptidoglycan lytic amidase}},
url = {{http://dx.doi.org/10.1002/pro.4585}},
doi = {{10.1002/pro.4585}},
volume = {{32}},
year = {{2023}},
}