Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: EC:3.5.1.4 (deaminase)
 5,113 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The enzymes of the mandelate metabolic pathway permit Pseudomonas putida ATCC 12633 to utilize either or both enantiomers of mandelate as the sole carbon source. The genes encoding the mandelate pathway were found to lie on a single 10.5-kb restriction fragment. Part of that fragment was shown to contain the genes coding for mandelate racemase, mandelate dehydrogenase, and benzoylformate decarboxylase arranged in an operon. Here we report the sequencing of the remainder of the restriction fragment, which revealed three further open reading frames, denoted mdlX, mdlY, and mdlD. All were transcribed in the opposite direction from the genes of the mdlABC operon. Sequence alignments suggested that the open reading frames encoded a regulatory protein (mdlX), a member of the amidase signature family (mdlY), and an NAD(P)(+)-dependent dehydrogenase (mdlD). The mdlY and mdlD genes were isolated and expressed in Escherichia coli, and the purified gene products were characterized as a mandelamide hydrolase and an NAD(P)(+)-dependent benzaldehyde dehydrogenase, respectively.
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PMID:Identification and characterization of a mandelamide hydrolase and an NAD(P)+-dependent benzaldehyde dehydrogenase from Pseudomonas putida ATCC 12633. 1267 Sep 68

Benzyl alcohol is a naturally occurring aromatic alcohol and has been widely used in the cosmetics and flavor/fragrance industries. The whole-cell biotransformation for synthesis of benzyl alcohol directly from bio-based L-phenylalanine (L-Phe) was herein explored using an artificial enzyme cascade in Escherichia coli. Benzaldehyde was first produced from L-Phe via four heterologous enzymatic steps that comprises L-amino acid deaminase (LAAD), hydroxymandelate synthase (HmaS), (S)-mandelate dehydrogenase (SMDH) and benzoylformate decarboxylase (BFD). The subsequent reduction of benzaldehyde to benzyl alcohol was achieved by a broad substrate specificity phenylacetaldehyde reductase (PAR) from Solanum lycopersicum. We found the designed enzyme cascade could efficiently convert L-Phe into benzyl alcohol with conversion above 99%. In addition, we also examined L-tyrosine (L-Tyr) and m-fluoro-phenylalanine (m-f-Phe) as substrates, the cascade biotransformation could also efficiently produce p-hydroxybenzyl alcohol and m-fluoro-benzyl alcohol. In summary, the developed biocatalytic pathway has great potential to produce various high-valued fine chemicals.
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PMID:One-Pot Cascade Biotransformation for Efficient Synthesis of Benzyl Alcohol and Its Analogs. 3201 96