Dual Activity BLEG-1 from Bacillus lehensis G1 Revealed Structural Resemblance to B3 Metallo-β-Lactamase and Glyoxalase II: An Insight into Its Enzyme …

SX Au, NS Dzulkifly, ND Muhd Noor… - International Journal of …, 2021 - mdpi.com
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 …

Probing the substrate binding modes and catalytic mechanisms of BLEG-1, a promiscuous B3 metallo-β-lactamase with glyoxalase II properties

SX Au, A Mohd Padzil, ND Muhd Noor, H Matsumura… - Plos one, 2023 - journals.plos.org
BLEG-1 from Bacillus lehensis G1 is an evolutionary divergent B3 metallo-β-lactamase
(MBL) that exhibited both β-lactamase and glyoxalase II (GLXII) activities. Sequence …

Danger lurking in the “unknowns”: structure-to-function studies of hypothetical protein Bleg1_2437 from Bacillus lehensis G1 alkaliphile revealed an evolutionary …

SH Tan, YM Normi, ATC Leow, AB Salleh… - The journal of …, 2017 - academic.oup.com
The effectiveness of β-lactam antibiotics as chemotherapeutic agents to treat bacterial
infections is gradually threatened with the emergence of antibiotic resistance mechanism …

Design and characterisation of inhibitory peptides against Bleg1_2478, an evolutionary divergent B3 metallo-β-lactamase

G Selvaraju, TC Leow, AB Salleh, YM Normi - Molecules, 2020 - mdpi.com
Previously, a hypothetical protein (HP) termed Bleg1_2437 (currently named Bleg1_2478)
from Bacillus lehensis G1 was discovered to be an evolutionary divergent B3 subclass …

Structural and biochemical characterization of Rm3, a subclass B3 metallo-β-lactamase identified from a functional metagenomic study

R Salimraj, L Zhang, P Hinchliffe… - Antimicrobial agents …, 2016 - Am Soc Microbiol
ABSTRACT β-Lactamase production increasingly threatens the effectiveness of β-lactams,
which remain a mainstay of antimicrobial chemotherapy. New activities emerge through both …

Structural Insights for Core Scaffold and Substrate Specificity of B1, B2, and B3 Metallo-β-Lactamases

Y Yun, S Han, YS Park, H Park, D Kim, Y Kim… - Frontiers in …, 2022 - frontiersin.org
Metallo-β-lactamases (MBLs) hydrolyze almost all β-lactam antibiotics, including penicillins,
cephalosporins, and carbapenems; however, no effective inhibitors are currently clinically …

Biochemical and genetic characterization of a novel metallo-β-lactamase from marine bacterium Erythrobacter litoralis HTCC 2594

XW Jiang, H Cheng, YY Huo, L Xu, YH Wu, WH Liu… - Scientific reports, 2018 - nature.com
Abstract Metallo-β-lactamases (MBLs) are a group of enzymes that can inactivate most
commonly used β-lactam-based antibiotics. Among MBLs, New Delhi metallo-β-lactamase-1 …

Dual activity of PNGM-1 pinpoints the evolutionary origin of subclass B3 metallo-β-lactamases: a molecular and evolutionary study

JH Lee, M Takahashi, JH Jeon, LW Kang… - Emerging microbes & …, 2019 - Taylor & Francis
Resistance to β-lactams is one of the most serious problems associated with Gram-negative
infections. β-Lactamases are able to hydrolyze β-lactams such as cephalosporins and/or …

Kinetic and structural characterization of the first B3 metallo-β-lactamase with an active-site glutamic acid

LA Wilson, EG Knaven, MT Morris… - Antimicrobial agents …, 2021 - Am Soc Microbiol
The structural diversity in metallo-β-lactamases (MBLs), especially in the vicinity of the active
site, has been a major hurdle in the development of clinically effective inhibitors …

Broad antibiotic resistance profile of the subclass B3 metallo‐β‐lactamase GOB‐1, a di‐zinc enzyme

LE Horsfall, Y Izougarhane, P Lassaux… - The FEBS …, 2011 - Wiley Online Library
The metallo‐β‐lactamase (MBL) GOB‐1 was expressed via a T7 expression system in
Escherichia coli BL21 (DE3). The MBL was purified to homogeneity and shown to exhibit a …