Dual activity bleg-1 from Bacillus Lehensis g1 revealed structural resemblance to b3 metallo-β-lactamase and glyoxalase ii: An insight into its enzyme promiscuity and evolutionary divergence
Metallo-β-lactamases (MBLs) are class B β-lactamases from the metallo-hydrolase-like MBL-fold superfamily which act on a broad range of β-lactam antibiotics. A previous study on BLEG-1 (formerly called Bleg1_2437), a hypothetical protein from Bacillus lehensis G1, revealed sequence similarity and ac...
Saved in:
Main Authors: | , , , , , |
---|---|
Format: | Article |
Published: |
Multidisciplinary Digital Publishing Institute
2021
|
Online Access: | http://psasir.upm.edu.my/id/eprint/96804/ https://www.mdpi.com/1422-0067/22/17/9377 |
Tags: |
Add Tag
No Tags, Be the first to tag this record!
|
id |
my.upm.eprints.96804 |
---|---|
record_format |
eprints |
spelling |
my.upm.eprints.968042023-04-19T04:09:08Z http://psasir.upm.edu.my/id/eprint/96804/ Dual activity bleg-1 from Bacillus Lehensis g1 revealed structural resemblance to b3 metallo-β-lactamase and glyoxalase ii: An insight into its enzyme promiscuity and evolutionary divergence Au, Shaw Xian Dzulkifly, Nur Syazana Muhd Noor, Noor Dina Matsumura, Hiroyoshi Raja Abdul Rahman, Raja Noor Zaliha Mohd Yahaya, Normi Metallo-β-lactamases (MBLs) are class B β-lactamases from the metallo-hydrolase-like MBL-fold superfamily which act on a broad range of β-lactam antibiotics. A previous study on BLEG-1 (formerly called Bleg1_2437), a hypothetical protein from Bacillus lehensis G1, revealed sequence similarity and activity to B3 subclass MBLs, despite its evolutionary divergence from these enzymes. Its relatedness to glyoxalase II (GLXII) raises the possibility of its enzymatic promiscuity and unique structural features compared to other MBLs and GLXIIs. This present study highlights that BLEG-1 possessed both MBL and GLXII activities with similar catalytic efficiencies. Its crystal structure revealed highly similar active site configuration to YcbL and GloB GLXIIs from Salmonella enterica, and L1 B3 MBL from Stenotrophomonas maltophilia. However, different from GLXIIs, BLEG-1 has an insertion of an active-site loop, forming a binding cavity similar to B3 MBL at the N-terminal region. We propose that BLEG-1 could possibly have evolved from GLXII and adopted MBL activity through this insertion. Multidisciplinary Digital Publishing Institute 2021 Article PeerReviewed Au, Shaw Xian and Dzulkifly, Nur Syazana and Muhd Noor, Noor Dina and Matsumura, Hiroyoshi and Raja Abdul Rahman, Raja Noor Zaliha and Mohd Yahaya, Normi (2021) Dual activity bleg-1 from Bacillus Lehensis g1 revealed structural resemblance to b3 metallo-β-lactamase and glyoxalase ii: An insight into its enzyme promiscuity and evolutionary divergence. International Journal of Molecular Sciences, 22 (17). art. no. 9377. pp. 1-21. ISSN 1661-6596; ESSN: 1422-0067 https://www.mdpi.com/1422-0067/22/17/9377 10.3390/ijms22179377 |
institution |
Universiti Putra Malaysia |
building |
UPM Library |
collection |
Institutional Repository |
continent |
Asia |
country |
Malaysia |
content_provider |
Universiti Putra Malaysia |
content_source |
UPM Institutional Repository |
url_provider |
http://psasir.upm.edu.my/ |
description |
Metallo-β-lactamases (MBLs) are class B β-lactamases from the metallo-hydrolase-like MBL-fold superfamily which act on a broad range of β-lactam antibiotics. A previous study on BLEG-1 (formerly called Bleg1_2437), a hypothetical protein from Bacillus lehensis G1, revealed sequence similarity and activity to B3 subclass MBLs, despite its evolutionary divergence from these enzymes. Its relatedness to glyoxalase II (GLXII) raises the possibility of its enzymatic promiscuity and unique structural features compared to other MBLs and GLXIIs. This present study highlights that BLEG-1 possessed both MBL and GLXII activities with similar catalytic efficiencies. Its crystal structure revealed highly similar active site configuration to YcbL and GloB GLXIIs from Salmonella enterica, and L1 B3 MBL from Stenotrophomonas maltophilia. However, different from GLXIIs, BLEG-1 has an insertion of an active-site loop, forming a binding cavity similar to B3 MBL at the N-terminal region. We propose that BLEG-1 could possibly have evolved from GLXII and adopted MBL activity through this insertion. |
format |
Article |
author |
Au, Shaw Xian Dzulkifly, Nur Syazana Muhd Noor, Noor Dina Matsumura, Hiroyoshi Raja Abdul Rahman, Raja Noor Zaliha Mohd Yahaya, Normi |
spellingShingle |
Au, Shaw Xian Dzulkifly, Nur Syazana Muhd Noor, Noor Dina Matsumura, Hiroyoshi Raja Abdul Rahman, Raja Noor Zaliha Mohd Yahaya, Normi Dual activity bleg-1 from Bacillus Lehensis g1 revealed structural resemblance to b3 metallo-β-lactamase and glyoxalase ii: An insight into its enzyme promiscuity and evolutionary divergence |
author_facet |
Au, Shaw Xian Dzulkifly, Nur Syazana Muhd Noor, Noor Dina Matsumura, Hiroyoshi Raja Abdul Rahman, Raja Noor Zaliha Mohd Yahaya, Normi |
author_sort |
Au, Shaw Xian |
title |
Dual activity bleg-1 from Bacillus Lehensis g1 revealed structural resemblance to b3 metallo-β-lactamase and glyoxalase ii: An insight into its enzyme promiscuity and evolutionary divergence |
title_short |
Dual activity bleg-1 from Bacillus Lehensis g1 revealed structural resemblance to b3 metallo-β-lactamase and glyoxalase ii: An insight into its enzyme promiscuity and evolutionary divergence |
title_full |
Dual activity bleg-1 from Bacillus Lehensis g1 revealed structural resemblance to b3 metallo-β-lactamase and glyoxalase ii: An insight into its enzyme promiscuity and evolutionary divergence |
title_fullStr |
Dual activity bleg-1 from Bacillus Lehensis g1 revealed structural resemblance to b3 metallo-β-lactamase and glyoxalase ii: An insight into its enzyme promiscuity and evolutionary divergence |
title_full_unstemmed |
Dual activity bleg-1 from Bacillus Lehensis g1 revealed structural resemblance to b3 metallo-β-lactamase and glyoxalase ii: An insight into its enzyme promiscuity and evolutionary divergence |
title_sort |
dual activity bleg-1 from bacillus lehensis g1 revealed structural resemblance to b3 metallo-β-lactamase and glyoxalase ii: an insight into its enzyme promiscuity and evolutionary divergence |
publisher |
Multidisciplinary Digital Publishing Institute |
publishDate |
2021 |
url |
http://psasir.upm.edu.my/id/eprint/96804/ https://www.mdpi.com/1422-0067/22/17/9377 |
_version_ |
1765298659859103744 |
score |
13.18916 |