Molecular Basis of Cysteine Biosynthesis in Plants STRUCTURAL AND FUNCTIONAL ANALYSIS OF O-ACETYLSERINE SULFHYDRYLASE FROM ARABIDOPSIS THALIANA

Ammonia-lyases and aminomutases are mechanistically and structurally diverse enzymes which catalyze the deamination and/or isomerization of amino acids in nature by cleaving or shifting a C–N bond. Of the many protein families in which these enzyme activities are found, only a subset have been employed in the synthesis of optically pure fine chemicals or in medical applications. This review covers the natural diversity of these enzymes, highlighting particular enzyme classes that are used within industrial and medical biotechnology. These highlights detail the discovery and mechanistic investigations of these commercially relevant enzymes, along with comparisons of their various applications as stand-alone catalysts, components of artificial biosynthetic pathways and biocatalytic or chemoenzymatic cascades, and therapeutic tools for the potential treatment of various pathologies.

/pdf/synthetic-and-therapeutic-applications-of-ammonia-lyases-and-1822044iwn.pdf

Synthetic and Therapeutic Applications of Ammonia-lyases and Aminomutases

https://biochem.slu.edu/faculty/dicera_new/dicera_files/jbc06_dicera.pdf

A Structural Perspective on Enzymes Activated by Monovalent Cations

Crystal Structure of a Homolog of Mammalian Serine Racemase from Schizosaccharomyces pombe

Natural product discovery efforts have focused primarily on microbial biosynthetic gene clusters (BGCs) containing large multimodular polyketide synthases and nonribosomal peptide synthetases; however, sequencing of fungal genomes has revealed a vast number of BGCs containing smaller NRPS-like genes of unknown biosynthetic function. Using comparative metabolomics, we show that a BGC in the human pathogen Aspergillus fumigatus named fsq, which contains an NRPS-like gene lacking a condensation domain, produces several new isoquinoline alkaloids known as the fumisoquins. These compounds derive from carbon-carbon bond formation between two amino acid-derived moieties followed by a sequence that is directly analogous to isoquinoline alkaloid biosynthesis in plants. Fumisoquin biosynthesis requires the N-methyltransferase FsqC and the FAD-dependent oxidase FsqB, which represent functional analogs of coclaurine N-methyltransferase and berberine bridge enzyme in plants. Our results show that BGCs containing incomplete NRPS modules may reveal new biosynthetic paradigms and suggest that plant-like isoquinoline biosynthesis occurs in diverse fungi.

Plant-like biosynthesis of isoquinoline alkaloids in Aspergillus fumigatus

SDH (l-serine dehydratase, EC 4.3.1.17) catalyzes the pyridoxal 5‘-phosphate (PLP)-dependent dehydration of l-serine to yield pyruvate and ammonia. Liver SDH plays an important role in gluconeogenesis. Formation of pyruvate by SDH is a two-step reaction in which the hydroxyl group of serine is cleaved to produce aminoacrylate, and then the aminoacrylate is deaminated by nonenzymatic hydrolysis to produce pyruvate. The crystal structure of rat liver apo-SDH was determined by single isomorphous replacement at 2.8 A resolution. The holo-SDH crystallized with O-methylserine (OMS) was also determined at 2.6 A resolution by molecular replacement. SDH is composed of two domains, and each domain has a typical αβ-open structure. The active site is located in the cleft between the two domains. The holo-SDH contained PLP−OMS aldimine in the active site, indicating that OMS can form the Schiff base linkage with PLP, but the subsequent dehydration did not occur. Apo-SDH forms a dimer by inserting the small domain into...

Crystal structure of serine dehydratase from rat liver.

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Crystal structure of serine dehydratase from rat liver.