Journal: Applied Microbiology and Biotechnology

Article Title: Novel oleate hydratases and potential biotechnological applications

doi: 10.1007/s00253-021-11465-x

Figure Lengend Snippet: Overview of biocatalytic cascades with Ohy. FAP, fatty acid photodecarboxylase; ATA, amine transaminase; BVMO, Baeyer-Villiger monooxygenase. a Oleate hydratase-catalysed hydration of oleic acid to 10-hydroxystearic acid, b FAP-catalysed decarboxylation of 10-HSA to 9-hydroxy heptadecane, c lipase-catalysed esterification of 10-HSA to the FAHFA 10-[(1-oxohexadecyl)oxy]-octadecanoic acid, d secondary alcohol dehydrogenase-catalysed oxidation of 10-HSA to 10-ketostearic acid, e transamination catalysed by amine transaminase of 10-ketostearic acid to 10-aminostearic acid, f decarboxylation of 10-aminostearic acid to 9-amino heptadecane, g BVMO-catalysed oxidation of 10-ketostearic acid to 1- O -octyl decanedioate, h BVMO-catalysed oxidation of 10-ketostearic acid to 9-octanoyloxy nonanoic acid, i FAP-catalysed decarboxylation of 9-octanoyloxy nonanoic acid to octyl octanoate, j esterase-catalysed hydrolysis of 1- O -octyl decanedioate to n -octanol and 1,10-decanedioic acid, k esterase-catalysed hydrolysis of 9-octanoyloxy nonanoic acid to octanoic acid and 9-hydroxynonanoic acid, and l esterase-catalysed hydrolysis of octyl octanoate to octanoic acid and n -octanol

Article Snippet: An extensive bioinformatic study to discover and analyse Ohy coding sequences using the BioCatNet database system resulted in the construction of the hydratase engineering database HyED ( https://hyed.biocatnet.de/ ) which contains more than 2000 unique sequences (Schmid et al. ).

Techniques:

Journal: Applied Microbiology and Biotechnology

Article Title: On the current role of hydratases in biocatalysis

doi: 10.1007/s00253-018-9065-7

Figure Lengend Snippet: Typical water addition reactions to non-activated carbon-carbon double bonds catalysed by hydratases. FAH = fatty acid hydratase; KHS = kievitone hydratase; LDI = linalool dehydratase-isomerase; CrtC and CruF = carotenoid-1,2-hydratases; LIH = limonene hydratase; ACH = acetylene hydratase; PAD = phenolic acid decarboxylase; FDC = ferulic acid decarboxylase. The asterisk in the ACH catalysed hydration of acetylene indicates hydration of a carbon-carbon triple bond

Article Snippet: Recently, the amino acid sequences of 2046 putative FAHs were allocated to 11 homologous families (HFam1–11) in a hydratase engineering database (HyED) (Schmid et al. ).

Techniques:

Journal: Applied Microbiology and Biotechnology

Article Title: On the current role of hydratases in biocatalysis

doi: 10.1007/s00253-018-9065-7

Figure Lengend Snippet: Active site architectures and proposed reaction mechanisms of hydratases catalysing water addition to non-activated carbon-carbon double and triple bonds. a Active site of Elizabethkingia meningoseptica oleate hydratase (OhyA; PDB-code: 4UIR) with docked oleic acid in grey, FAD in yellow and catalytic residues in light orange (Engleder et al. ). b Active site of Castelaniella defragrans linalool dehydratase-isomerase (LDI; PDB-code: 5HSS) with co-crystallised β - myrcene in orange and catalytic residues in magenta (Weidenweber et al. ). c Active site of Pelobacter acetylenicus acetylene hydratase (ACH; PDB-code: 2E7Z) showing both MGD cofactors and the tightly coordinated tungsten (blue), as well as the [4Fe:4S] cluster and the catalytic aspartate (Seiffert et al. 2007). ( d ) Active site of Enterobacter sp. ferulic acid decarboxylase (PAD; PDB-code: 3NX2) in complex with 3-(4-hydroxy-3-methoxyphenyl)-2-propenoic acid (dark blue) and residues important for substrate binding (light brown) and catalysis (Gu et al. )

Article Snippet: Recently, the amino acid sequences of 2046 putative FAHs were allocated to 11 homologous families (HFam1–11) in a hydratase engineering database (HyED) (Schmid et al. ).

Techniques: Binding Assay