Organophosphorus acid anhydrolase fromAlteromonas macleodii: structural study and functional relationship to prolidases

Abstract

The bacterial enzyme organophosphorus acid anhydrolase (OPAA) is able to catalyze the hydrolysis of both proline dipeptides (Xaa-Pro) and several types of organophosphate (OP) compounds. The full three-dimensional structure of the manganese-dependent OPAA enzyme is presented for the first time. This enzyme, which was originally isolated from the marine bacterium Alteromonas macleodii, was prepared recombinantly in Escherichia coli. The crystal structure was determined at 1.8 Å resolution in space group C2, with unit-cell parameters a = 133.8, b = 49.2, c = 97.3 Å, β = 125.0°. The enzyme forms dimers and their existence in solution was confirmed by dynamic light scattering and size-exclusion chromatography. The enzyme shares the pita-bread fold of its C-terminal domain with related prolidases. The binuclear manganese centre is located in the active site within the pita-bread domain. Moreover, an Ni(2+) ion from purification was localized according to anomalous signal. This study presents the full structure of this enzyme with complete surroundings of the active site and provides a critical analysis of its relationship to prolidases.

Enzymatic and proteomic exploration into the inhibitory activities of lemongrass and lemon essential oils against Botrytis cinerea (causative pathogen of gray mold)

“…Prolidase has been shown to contribute to osmoregulation by releasing free proline ( Zaprasis et al, 2013 ), and prolidase variations have been linked to antibiotic resistance ( Wilk et al, 2021 ). Prolidases are believed to have a broad antitoxin protective role due to their capacity to hydrolyse organophosphorus chemicals ( Štěpánková et al, 2013 ). It is noteworthy that the activities of prolidase in B. cinerea is not entirely understood, and the mechanism of inhibiting B. cinerea growth by Le is still unclear.…”

Biochemical Characterization of a Novel Alkaline-Tolerant Xaa-Pro Dipeptidase from Aspergillus phoenicis

“…Among them, the prolidase from Aureohacterium esteraromaticum [31] is possibly not a prolidase since it lacks the corresponding active site and metal-binding residues of prolidases as shown by multiple sequence alignment. Previously, prokaryotic prolidases have been classified into two subfamilies (XPDxc-type and XPD48-type) according to their molecular weights and sequence relatedness [4,9,29]. However, this classification system may cause confusion, as observed for prolyl aminopeptidases [32].…”

“…Organophosphorus (OP) cholinesterase-inhibiting compounds are constituents of many chemical nerve agents and pesticides. Some XPDs also exhibit OPAA activity and can detoxify these OP compounds by cleaving the P-F and P-O bonds, and this ability allows them to serve as biosensors or environmentally friendly decontaminating agents to detect/degrade OP pesticides and chemical warfare nerve agents [9,10]. Currently, several approaches, such as immobilization [11] and protein engineering [12,13], have also been adopted to improve the OPAA activities of several XPDs.…”

The Organophosphate Degradation (opd) Island-borne Esterase-induced Metabolic Diversion in Escherichia coli and Its Influence on p-Nitrophenol Degradation

“…The PTEs have been classified into three main groups: (i) the organophosphate hydrolases (OPHs), (ii) methyl parathion hydrolases (MPHs), and (iii) organophosphate acid anhydrases. Among the PTEs, only the organophosphate acid anhydrases have known physiological substrates: they have been shown to be dipeptidases that cleave dipeptides with a prolyl residue at the carboxyl terminus and hence are described as prolidases (3). The OP hydrolyzing activity of prolidases is considered to be an ancillary activity due to the structural similarity of OP compounds to their usual substrates (3).…”

“…Bacterial phosphotriesterases (PTEs) 3 are a group of structurally unrelated enzymes that cleave the triester linkage found in both organophosphate (OP) insecticides and OP nerve agents (1). Because of their broad substrate range and high catalytic efficiency, they have been exploited for detection and decontamination of OP compounds (2).…”