ACC Deaminase from <i>Lysobacter gummosus</i> OH17 Can Promote Root Growth in <i>Oryza sativa</i> Nipponbare Plants

Although <i>Lysobacter</i> species are a remarkable source of natural compounds with antibacterial and antifungal activities, the ability of these bacteria to produce plant growth promoters remains practically unknown. In this work, the ethylene precursor 1-aminocyclopropane-1-carboxylic acid (ACC) has been isolated from the secretions of <i>Lysobacter gummosus</i> OH17, indicating the presence of an ACC deaminase, which was shown to be encoded in the gene <i>peg_1256</i>. The recombinant enzyme could not only deaminate ACC to provide 2-oxobutanoic acid but also catalyzed the amination of the 2-oxobutanoic acid, demonstrating, for the first time, that ACC deaminases can produce ACC. After the treatment of rice <i>Oryza sativa</i> Nipponbare plants with OH17 ACC deaminase, the ethylene production levels were 44% higher in comparison with the control experiments, allowing significant improvements in root, 10%, and stem, 14%, growth

Production of Antifungal <i>p</i>‑Aminobenzoic Acid in <i>Lysobacter antibioticus</i> OH13

Among <i>Lysobacter</i> species, <i>Lysobacter antibioticus</i> has been demonstrated to be an interesting source of antimicrobial metabolites for the biocontrol of plant diseases. Although the antibacterial activity was attributed to <i>N</i>-oxide phenazines, the active compounds involved in the antifungal function remained unknown. In this work, an antifungal compound was isolated and identified as <i>p</i>-aminobenzoic acid (pABA). Antifungal activity screening revealed that pABA shows activity against a number of plant pathogens. The genes involved in the synthetic route of this compound in OH13 were identified. Further, the production of pABA was optimized by modification of the carbon source using engineered <i>L. antibioticus</i> OH13 strains

Aldolase-Catalyzed Synthesis of Conformationally Constrained Iminocyclitols: Preparation of Polyhydroxylated Benzopyrrolizidines and Cyclohexapyrrolizidines

A straightforward chemo-enzymatic synthesis of new polyhydroxylated benzo­pyrrolizidines and cyclo­hexa­pyrrolizidines is developed. The two-step strategy consists of l-fuculose-1-phosphate aldolase variant F131A-catalyzed aldol addition of dihydroxy­acetone phosphate to <i>rac</i>-<i>N</i>-benzyl­oxycarbonyl­indoline-2-carb­aldehyde as well as (2<i>S</i>*,3a<i>S</i>*,7a<i>S</i>*)- and (2<i>S</i>*,3a<i>R</i>*,7a<i>R</i>*)-<i>N</i>-benzyl­oxycarbonyl­octa­hydro­indole-2-carb­aldehydes and a subsequent one-step catalytic deprotection–reductive amination

Dynamic Kinetic Resolution of 1,3-Dihydro-2<i>H</i>-isoindole-1-carboxylic Acid Methyl Ester: Asymmetric Transformations toward Isoindoline Carbamates

Asymmetric syntheses of isoindoline carbamates have been successfully achieved through enzyme-mediated dynamic kinetic resolution processes and without requirement of metal or acid–base catalyst for the substrate racemization. Optically active carbamates were obtained in good yields and an excellent degree of stereoselectivity when <i>Pseudomonas cepacia</i> lipase (PSL) was used as biocatalyst, with diallyl or dibenzyl carbonates being both adequate reagents in alkoxycarbonylation reactions

Dynamic Kinetic Resolution of 1,3-Dihydro-2<i>H</i>-isoindole-1-carboxylic Acid Methyl Ester: Asymmetric Transformations toward Isoindoline Carbamates

Asymmetric syntheses of isoindoline carbamates have been successfully achieved through enzyme-mediated dynamic kinetic resolution processes and without requirement of metal or acid–base catalyst for the substrate racemization. Optically active carbamates were obtained in good yields and an excellent degree of stereoselectivity when <i>Pseudomonas cepacia</i> lipase (PSL) was used as biocatalyst, with diallyl or dibenzyl carbonates being both adequate reagents in alkoxycarbonylation reactions