A novel family of bacterial dioxygenases that catalyse the hydroxylation of free l-amino acids

Smirnov, Sergey V.; Sokolov, Pavel M.; Kodera, Tomohiro; Sugiyama, Masakazu; Hibi, Makoto; Shimizu, Sakayu; Yokozeki, Kenzo; Ogawa, Jun

doi:10.1111/j.1574-6968.2012.02558.x

Cited by 30 publications

(35 citation statements)

References 24 publications

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“…Previously, we found that HilB from Pantoea ananatis AJ13355 also catalyzes the C‐4‐hydroxylation of l ‐isoleucine, but the K M value deduced from the kinetic analysis of this reaction was much greater than that determined for IDO, suggesting that l ‐isoleucine is not a natural substrate of HilB (Smirnov et al. ). In contrast to IDO, HilB is coexpressed with a putative dioxygenase, HilA.…”

Section: Introductionmentioning

confidence: 84%

“…l ‐leucine, l ‐isoleucine, and l ‐threonine were found to be hydroxylated by the PF10014 members, producing 4‐hydroxyleucine, 4‐hydroxyisoleucine, and 4‐hydroxythreonine, respectively (Smirnov et al. ). A detailed analysis of the genetic organization of PF10014 members revealed a unique operon structure (designated the Hil operon, from the h ydroxylation of i so l eucine) in the genomes of several gram‐negative plant pathogens belonging to the Pantoea and Pseudomonas genera (Smirnov et al.…”

Section: Introductionmentioning

confidence: 99%

“…A detailed analysis of the genetic organization of PF10014 members revealed a unique operon structure (designated the Hil operon, from the h ydroxylation of i so l eucine) in the genomes of several gram‐negative plant pathogens belonging to the Pantoea and Pseudomonas genera (Smirnov et al. ) (Fig. ).…”

Section: Introductionmentioning

confidence: 99%

“…2e2 (Smirnov et al. ); (B) Pantoea ananatis AJ 13355 (Hara et al. ), P. ananatis LMG 20103 (De Maayer et al.…”

Section: Introductionmentioning

confidence: 99%

“…The distinguishing feature of the Hil operon is the presence of a “core” of five genes: HilR – a putative LysR‐type transcriptional regulator (Pfam family PF 00126) (Schell ); HilP – a putative extracellular solute‐binding protein ( PF 00497); HilA – a putative dioxygenase ( PF 13640); HilB – a dioxygenase ( PF 10014) that is a close homologue of l ‐isoleucine‐4‐dioxygenase ( IDO ) (Smirnov et al. ); and HilC – a short‐chain dehydrogenase ( PF 00106) that is a close homologue of 2‐amino‐3‐methyl‐4‐ketopentanoic acid ( AMKP ) reductase ( AR ). Other genes included in the Hil operon are bacterium specific: RhtA – putative exporters belonging to the RhtA family (Livshits et al.…”

Section: Introductionmentioning

confidence: 99%

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A novel l‐isoleucine‐4′‐dioxygenase and l‐isoleucine dihydroxylation cascade in Pantoea ananatis

et al. 2013

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A unique operon structure has been identified in the genomes of several plant- and insect-associated bacteria. The distinguishing feature of this operon is the presence of tandem hilA and hilB genes encoding dioxygenases belonging to the PF13640 and PF10014 (BsmA) Pfam families, respectively. The genes encoding HilA and HilB from Pantoea ananatis AJ13355 were cloned and expressed in Escherichia coli. The culturing of E. coli cells expressing hilA (E. coli-HilA) or both hilA and hilB (E. coli-HilAB) in the presence of l-isoleucine resulted in the conversion of l-isoleucine into two novel biogenic compounds: l-4′-isoleucine and l-4,4′-dihydroxyisoleucine, respectively. In parallel, two novel enzymatic activities were detected in the crude cell lysates of the E. coli-HilA and E. coli-HilAB strains: l-isoleucine, 2-oxoglutarate: oxygen oxidoreductase (4′-hydroxylating) (HilA) and l-4′-hydroxyisoleucine, 2-oxoglutarate: oxygen oxidoreductase (4-hydroxylating) (HilB), respectively. Two hypotheses regarding the physiological significance of C-4(4′)-hydroxylation of l-isoleucine in bacteria are also discussed. According to first hypothesis, the l-isoleucine dihydroxylation cascade is involved in synthesis of dipeptide antibiotic in P. ananatis. Another unifying hypothesis is that the C-4(4′)-hydroxylation of l-isoleucine in bacteria could result in the synthesis of signal molecules belonging to two classes: 2(5H)-furanones and analogs of N-acyl homoserine lactone.

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Section: Introductionmentioning

confidence: 84%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

“…2e2 (Smirnov et al. ); (B) Pantoea ananatis AJ 13355 (Hara et al. ), P. ananatis LMG 20103 (De Maayer et al.…”

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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A novel l‐isoleucine‐4′‐dioxygenase and l‐isoleucine dihydroxylation cascade in Pantoea ananatis

et al. 2013

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Synthesis of Mono‐ and Dihydroxylated Amino Acids with New α‐Ketoglutarate‐Dependent Dioxygenases: Biocatalytic Oxidation of CH Bonds

et al. 2014

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Iron(II)/α‐ketoacid‐dependent oxygenases (αKAOs) are enzymes that mainly catalyse hydroxylation reaction. By using a genomic approach combining sequence comparison and protein‐domain sharing, a set of 131 αKAO enzymes was prepared. The screening of various substrates revealed five new αKAOs. Four αKAOs were found to be active towards L‐lysine, L‐ornithine and L‐arginine with total regio‐ and stereoselectivities and yielding the corresponding 3‐ or 4‐hydroxyamino acids. The enzymatic cascade reaction with two stereoselective regiodivergent αKAOs enabled the synthesis of 3,4‐dihydroxy‐L‐lysine.

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Crystal structure of a member of a novel family of dioxygenases (PF10014) reveals a conserved cupin fold and active site

Grant

Chiu

et al. 2013

Proteins

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PF10014 is a novel family of 2-oxyglutarate-Fe2+-dependent dioxygenases that are involved in biosynthesis of antibiotics and regulation of biofilm formation, likely by catalyzing hydroxylation of free amino acids or other related ligands. The crystal structure of a PF10014 member from Methylibium petroleiphilum at 1.9 Å resolution shows strong structural similarity to cupin dioxygenases in overall fold and active site, despite very remote homology. However, one of the β-strands of the cupin catalytic core is replaced by a loop that displays conformational isomerism that likely regulates the active site.

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A novel family of bacterial dioxygenases that catalyse the hydroxylation of free l-amino acids

Cited by 30 publications

References 24 publications

A novel l‐isoleucine‐4′‐dioxygenase and l‐isoleucine dihydroxylation cascade in Pantoea ananatis

A novel l‐isoleucine‐4′‐dioxygenase and l‐isoleucine dihydroxylation cascade in Pantoea ananatis

Synthesis of Mono‐ and Dihydroxylated Amino Acids with New α‐Ketoglutarate‐Dependent Dioxygenases: Biocatalytic Oxidation of CH Bonds

Crystal structure of a member of a novel family of dioxygenases (PF10014) reveals a conserved cupin fold and active site

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