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Fig. 6. Molecular docking simulation. A in In silico approach on sequential and structural variability in oryzacystatin and its interaction with cysteine protease enzymes of insect

Fig. 6. Molecular docking simulation. A) root-mean-square deviation (RMSD) B) number of hydrogen bonds C) radius of gyration D) minimum distance of OC XI – cathepsin O2 like and OC V – cathepsin F like complexes. Red color line denotes OC V- cathepsin F like and black color line denotes OC XI- cathepsin O2 like. (For interpretation of the references to color in this figure legend, the reader is referred to the Web version of this article.)

Fig. 2 in In silico approach on sequential and structural variability in oryzacystatin and its interaction with cysteine protease enzymes of insect

Fig. 2. Unrooted phylogenetic tree of all the eleven oryzacystatin protein sequence constructed by maximum likelihood method with bootstrap value as 1000 cycles. Bootstrap values are indicated at each branch. Three major clusters have been witnessed and divided as cluster 1, cluster 2, cluster 3. Cluster 1 contains OC VI, OC VII, OC VIII and OC XI, cluster 2 contains OC X, OC IV and OC V, and cluster 3 contains OC III, OCXII, OC I and OC II. Different colors denote the chromosome number encoding OC. Blue color represents chromosome 1, green color represents chromosome 5, yellow color represents chromosome 4, orange color represents chromosome 3 and m´elange color represents chromosome 9. (For interpretation of the references to color in this figure legend, the reader is referred to the Web version of this article.)

Fig. 3 in In silico approach on sequential and structural variability in oryzacystatin and its interaction with cysteine protease enzymes of insect

Fig. 3. Motif and its arrangement on oryzacystatin proteins by MEME software. 10 different motifs were shown and each color signifies different non-overlapping motifs. (For interpretation of the references to color in this figure legend, the reader is referred to the Web version of this article.)

Fig. 1. Oryzacystatin I in In silico approach on sequential and structural variability in oryzacystatin and its interaction with cysteine protease enzymes of insect

Fig. 1. Oryzacystatin I (OC I) structure with tripartite wedge showing conserved regions with key interacting amino acid residues.

Fig. 7 in In silico approach on sequential and structural variability in oryzacystatin and its interaction with cysteine protease enzymes of insect

Fig. 7. Root-mean-square fluctuation of OC XI, OC V, cathepsin O2 like and cathepsin F like proteases. Red color represents OC XI, green color represents for OC V, black color represents for cathepsin O2 like protease, and blue color represents cathepsin F like proteases. black oval-shaped marks denote the interactive amino acid residues of OC XI (QVVQG (73–77)), OC V (QVVSG (99–103)), cathepsin O2 like (Q-170; C-176; H-315; N- 335), cathepsin F like (Q-337; C-343; H-479; N-505). (For interpretation of the references to color in this figure legend, the reader is referred to the Web version of this article.)

Fig. 4. Top 10 in In silico approach on sequential and structural variability in oryzacystatin and its interaction with cysteine protease enzymes of insect

Fig. 4. Top 10 protein-protein interaction of oryzacystatins and cysteine protease enzymes based on docking scores. A) OC XI – cathepsin B. B) OC II – cathepsin B. C) OC IV – cathepsin B. D) OC IV – cathepsin O2 like. E) OC III – cathepsin B. F) OC IV – caspase 1. G) OC I – cathepsin B. H) OC V – cathepsin F like. I) OC VI – cathepsin B. J) OC XI – cathepsin O2 like protease enzyme. The protease cathepsin B showed the interaction in the wedge region of OC I (G), OC II (B), OC III (E), OC IV (C), OC VI (I) and OC XI (A). OC IV showed higher docking score with caspase 1 (F) and cathepsin O2 like (D), similarly, OC V and OC XI interacted with cathepsin F like (H) and cathepsin O2 (J) like respectively. The hydrogen bond between the oryzacystatins and cysteine protease enzymes are shown in dotted line (—). Structural graphics were produced by using BIOVIA Discovery studio visualizer software, version 20.1.0.

Fig. 5 in Pyrrolyl 4-quinolone alkaloids from the mangrove endophytic fungus Penicillium steckii SCSIO 41025: Chiral resolution, configurational assignment, and enzyme inhibitory activities

Fig. 5. Molecular docking result of (+)-1 in α-glucosidase (PDB ID: 5NN8). (A) 3D structure of the enzyme docked with (+)-1. (B) Detail analysis of the 2D binding model of (+)-1 with the residues surrounding the binding pocket of α-glucosidase.

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Fig. 3 in Stabilization of dhurrin biosynthetic enzymes from Sorghum bicolor using a natural deep eutectic solvent

Fig. 3. NADES-based stabilization of the dhurrin biosynthetic enzymes. A) Illustration of proteoliposomes comprising the POR2B, CYP79A1, CYP71E1 and UGT85B1 reconstituted in liposomes composed of phospholipids extracted from etiolated sorghum seedlings (Metabolon). B) Recovery of activity upon storage of enzymes in NADES and glycerol compared to buffer upon dilution displayed as relative conversion of tyrosine for the Metabolon samples and conversion of cyanohydrin to dhurrin for the UGT85B1 samples. Values are mean of three technical replicates± SD. C) Stability of dhurrin biosynthetic enzymes stored at room temperature in aqueous buffer, NADES and glycerol. Samples were diluted in buffer prior to activity assay. Values are mean of three technical replicates ±SD and fitted to a double exponential decay. D) Bar plot showing relative activity of the enzymes following incubation at various temperatures for 30 min in aqueous buffer, NADES and glycerol. Samples were diluted in buffer prior to activity assay. All values are mean of three independent technical replicates ± SD.

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Fig. 2 in Stabilization of dhurrin biosynthetic enzymes from Sorghum bicolor using a natural deep eutectic solvent

Fig. 2. Dhurrin biosynthesis in the presence of different NADESs. A) Etiolated sorghum seedlings used for preparation of microsomes. B) Tyrosine conversion assay in microsomes at different NADES concentrations indicates an optimum at 5% NADES for both glucose:tartrate and glucose:malate. Values are mean of three technical replicates ± SD.

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Fig. 1 in Stabilization of dhurrin biosynthetic enzymes from Sorghum bicolor using a natural deep eutectic solvent

Fig. 1. Formation of NADES derived from natural occurring metabolites in plants. A) Chemical structures of D-glucose, tartaric acid, malic acid, choline, glycerol and dhurrin. Mixtures of these metabolites were tested for their ability to form NADES and their potential role in stabilizing the dhurrin biosynthetic enzymes. B) Stoichiometric mixture of glucose and tartrate constitute a NADES with significantly lowered melting point compared to the individual components. C) Biosynthetic pathway of the natural product dhurrin in S. bicolor.

Fig. 6 in A metallothionein type 2 from Avicennia marina binds to iron and mediates hydrogen peroxide balance by activation of enzyme catalase

Fig. 6. Growth curves and CAT activities for strains of control and R-AmMT2. (A) Growth curves of strains control and R-AmMT2 in the medium containing H2O2. (B) The CAT activities of control and R-AmMT2 in response to H2O2. expressing MT isoforms.

Fig. 7 in A metallothionein type 2 from Avicennia marina binds to iron and mediates hydrogen peroxide balance by activation of enzyme catalase

Fig. 7. The CAT activities in the extract of control strain after treatment with Apo/GST-AmMT and Fe2+/GST-AmMT.

Fig. 5 in A metallothionein type 2 from Avicennia marina binds to iron and mediates hydrogen peroxide balance by activation of enzyme catalase

Fig. 5. The confirmation of binding of Fe2+ to the recombinant and pure AmMT2 in vitro. (A) The reaction of the Fe2+/AmMT2 with DTNB. (B) The comparison between UV absorption spectra of each of Apo/GST-AmMT2 and the corresponding complex Fe2+/GST-AmMT2.

Fig. 1 in A metallothionein type 2 from Avicennia marina binds to iron and mediates hydrogen peroxide balance by activation of enzyme catalase

Fig. 1. Amino acid sequence and expression vector maps. (A) The amino acid sequence of AmMT2. (B) The map of pET41a-AmMT2 and pET41a. The positions of His. tag, S. tag and GST. tag are shown in gray boxes.

Fig. 2 in A metallothionein type 2 from Avicennia marina binds to iron and mediates hydrogen peroxide balance by activation of enzyme catalase

Fig. 2. SDS-PAGE analysis of GST and GST–AmMT2. (A) Total soluble proteins extracted from E. coli harboring pET41a and pET41a-AmMT2 at 0, 1, 2, 3 and 4 h after addition of IPTG. (B) The GST-OsMTI-2b was purified using affinity chromatography (lane P). The white arrows show the bands corresponding to GST and the black arrows show the band corresponding to GST-AmMT2.

Fig. 4 in A metallothionein type 2 from Avicennia marina binds to iron and mediates hydrogen peroxide balance by activation of enzyme catalase

Fig. 4. Metal concentration variation in the medium of strains Control and RAmMT2 between T1 (6 h after addition of metal and IPTG to medium) and T0 (starting point of addition of metal). The data represent the mean ± SD obtained from two independent experiments with two replicates.

Fig. 3 in A metallothionein type 2 from Avicennia marina binds to iron and mediates hydrogen peroxide balance by activation of enzyme catalase

Fig. 3. Effect of heterologous expression of GST-OsMTI-3a on the tolerance of E. coli to Cd2+, Zn2+, Ni2+ Cu2+ and Fe2+. The data are the mean of two independent, experiments with two replicates.

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Fig. 8 in Site-directed mutagenesis of β sesquiphellandrene synthase enhances enzyme promiscuity

Fig. 8. Proposed mechanisms for the conversion of FPP into sesquiterpene products catalysed by PmSTS WT and its mutants (L454G and L454A). The scheme is derived from the proposed mechanism of monoterpenes synthases (Gatto et al., 2015; Piechulla et al., 2016). The products generated by the PmSTSΔ24WT are shown in black. New products generated by mutant L454G and L454A in this study are shown in red. (For interpretation of the references to colour in this figure legend, the reader is referred to the Web version of this article.)

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Fig. 9 in Site-directed mutagenesis of β sesquiphellandrene synthase enhances enzyme promiscuity

Fig. 9. The homology modelling illustration of the active site of PmSTSΔ24WT and PmSTSΔ24L454G. The residue L454 and Y418 are shown as stick and coloured in purple and orange, respectively. (A) The side chain of the L454 provides steric hindrance, preventing the rotation of the Y418 toward the interior of the active site. (B) The mutation of L454G provide sufficient space to allow the Y418 to undergo rotation toward the interior of the active site and (C) thus allowing interaction with other amino acid in the active site. (For interpretation of the references to colour in this figure legend, the reader is referred to the Web version of this article.)