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Pseudomonas putida
Published in Martin Koller, The Handbook of Polyhydroxyalkanoates, 2020
Maria Tsampika Manoli, Natalia Tarazona, Aranzazu Mato, Beatriz Maestro, Jesús M. Sanz, Juan Nogales, M. Auxiliadora Prieto
The first intracellular mcl-PHA depolymerase was described in P. putida GPo1, and its enzymatic activity was confirmed in vivo on the defective phaZ mutant (GPo500), where PHA accumulated, and the mutant was not able to degrade the polymer in the stationary phase [46]. Similar experiments and conclusions were obtained from P. putida U and P. putida KT2442 [47–50]. The first biochemical characterization of an intracellular mcl-PHA depolymerase was realized for the PhaZ from P. putida KT2442 [48]. The PhaZ preferentially hydrolyzes mcl-PHA containing aliphatic and aromatic monomers. The enzyme behaves as a serine hydrolase that is inhibited by phenylmethylsulfonyl fluoride. The three-dimensional structure of PhaZ complex with a 3-hydroxyoctanoate dimer has been modeled. The enzyme presents an α/β hydrolase-type fold, a central core of an eight-stranded β-sheet and α-helices packed on both sides and capped with a lid structure (residues 133–192) built up from five α-helices connected by loops and covering a possible catalytic triad (Ser102, Asp221, and His248) near the “hinge” of the lid [48] (see Figure 4.4D). The binding surface of the core domain is highly hydrophobic, and the only polar residues surrounding the substrate are the catalytic triad and Asn35, which may take part in substrate recognition as described for the analogous Ser34 in the CumD hydrolase template [51]. Finally, the presence of a shallow surface across the core domain, followed by an elongated deep cavity facilitates the accommodation of mcl-hydrocarbon chains of the substrate [48].
In silico approach for identification of polyethylene terephthalate hydrolase (PETase)-like enzymes
Published in Bioremediation Journal, 2022
Poorvi Saini, Ananya Grewall, Sunila Hooda
The results obtained in the current study can serve as the basis for characterizing more efficient and highly specific plastic degrading enzymes for industrial application. In a similar line of work, SM14est enzyme was identified in Streptomyces sp. SM14 isolated from a soil sample was initially characterized using in silico screening methods and compared to the most efficient and substrate specific bacterial PET hydrolase enzyme, IsPETase (Almeida et al. 2019). Prediction of the three dimensional structure and other characteristics was performed and compared, which indicated a high similarity in the catalytic triad and the conserved serine hydrolase motif of the two enzymes. This activity of SM14est was further confirmed using a PCL plate clearing assay that proved the high efficiency of this enzyme (Almeida et al. 2019).
Iodine-mediated oxidative N–S bond formation: a facile one-pot synthetic approach to 1,2,4-benzothiadiazine 1,1-dioxides under transition metal-free conditions
Published in Journal of Sulfur Chemistry, 2023
Sümeyye Buran Uğur, Şengül Dilem Doğan
Benzothiadizine-3-one 1,1-dioxide derivatives, an important class of organic molecules for medicinal chemistry, are associated with a broad range of biological activities including antihypertensive [1], antimicrobial, antiviral [2,3], and antirheumatic [4] (Figure 1). They also exhibit ATP-sensitive potassium channel openers activity [5], impaired synaptic transmission of function, serine hydrolase inhibitory activity [6] and physico-chemical characteristics which facilitates the crossing of the blood–brain barrier (Figure 1).