[29] Arylformamidase from streptomyces parvulus

Katz, Edward; Brown, D.A.; Hitchcock, Michael

doi:10.1016/s0076-6879(87)42031-4

Cited by 6 publications

(8 citation statements)

References 22 publications

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“…Kynurenine formamidase has been isolated from many sources, including eukaryotic and prokaryotic organisms such as rat (Shinoara and Ishiguro, 1970), guinea pig (Santti andHopsu-Havu, 1968), chicken (Bayley andWagner, 1974), Drosophila melanogaster (Moore and Sullivan 1975), fish and cattle (Serrano and Nagayama, 1991), and Streptomycesparvolus (Brown et al, 1980(Brown et al, , 1986Katz et al, 1987). Two different forms of enzyme have been isolated and characterized: a higher-molecularweight form, formamidase I, and a lower-molecular-weight form, formamidase 11.…”

Section: B Aerobic Pathwaymentioning

confidence: 99%

“…Two different forms of enzyme have been isolated and characterized: a higher-molecularweight form, formamidase I, and a lower-molecular-weight form, formamidase 11. Most organisms possess only one of the two forms, whereas Drosophila melanoguster and Streptomyces pawulus possess both forms (Moore and Sullivan, 1975;Katz et al, 1987). In S. parvulus, formamidase I appears to be constitutive, whereas formamidase I1 is induced before antibiotic synthesis is initiated, thus playing a specific role for the specialized function of actinomycine formation.…”

Section: B Aerobic Pathwaymentioning

confidence: 99%

See 1 more Smart Citation

Enzymology of Nad ⁺ Synthesis

Magni

Amici

Emanuelli

et al. 1999

Advances in Enzymology - And Related Areas of Molecular Biology

194

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Section: B Aerobic Pathwaymentioning

confidence: 99%

Section: B Aerobic Pathwaymentioning

confidence: 99%

Enzymology of Nad ⁺ Synthesis

Magni

Amici

Emanuelli

et al. 1999

Advances in Enzymology - And Related Areas of Molecular Biology

194

View full text Add to dashboard Cite

“…This is also the case in S. chrysomallus, where the catabolic kynureninase gene kynU is flanked by genes that encode a tryptophan dioxygenase and a kynurenine formamidase (I. Crnovcic and U. Keller, unpublished data). Katz et al (35) reported two kynurenine formamidase enzymes in actinomycin-producing S. parvulus, one of which was formed at the onset of actinomycin production whereas the other was constitutive. Apparently, strain Sc-white possesses only the constitutive form.…”

Section: Resultsmentioning

confidence: 99%

“…In contrast, little is known about the genes that encode 4-MHA biosynthesis and the genes involved in regulation and self-resistance. It was shown previously that 4-MHA is derived from tryptophan (34), and enzymatic studies revealed pathway-specific isoforms of tryptophan oxygenase, kynurenine formamidase, and kynureninase activities in the actinomycin producers Streptomyces parvulus and S. chrysomallus (8,9,17,22,24,35,72). Moreover, an enzyme which methylates 3-hydroxyanthranilic acid (3-HA) at its 4 position was purified from S. antibioticus and character-.…”

mentioning

confidence: 99%

The Actinomycin Biosynthetic Gene Cluster ofStreptomyces chrysomallus: a Genetic Hall of Mirrors for Synthesis of a Molecule with Mirror Symmetry

et al. 2010

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A gene cluster was identified which contains genes involved in the biosynthesis of actinomycin encompassing 50 kb of contiguous DNA on the chromosome of Streptomyces chrysomallus. It contains 28 genes with biosynthetic functions and is bordered on both sides by IS elements. Unprecedentedly, the cluster consists of two large inverted repeats of 11 and 13 genes, respectively, with four nonribosomal peptide synthetase genes in the middle. Nine genes in each repeat have counterparts in the other, in the same arrangement but in the opposite orientation, suggesting an inverse duplication of one of the arms during the evolution of the gene cluster. All of the genes appear to be organized into operons, each corresponding to a functional section of actinomycin biosynthesis, such as peptide assembly, regulation, resistance, and biosynthesis of the precursor of the actinomycin chromophore 4-methyl-3-hydroxyanthranilic acid (4-MHA). For 4-MHA synthesis, functional analysis revealed genes that encode pathway-specific isoforms of tryptophan dioxygenase, kynurenine formamidase, and hydroxykynureninase, which are distinct from the corresponding enzyme activities of cellular tryptophan catabolism in their regulation and in part in their substrate specificity. Phylogenetic analysis indicates that the pathway-specific tryptophan metabolism in Streptomyces most probably evolved divergently from the normal pathway of tryptophan catabolism to provide an extra or independent supply of building blocks for the synthesis of tryptophan-derived secondary metabolites.

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“…The enzyme assay, based on an increase in optical density at 365 nm due to conversion of N ‐formyl‐ l ‐kynurenine to l ‐kynurenine, was adapted from [29]. The reaction mixture contained 100 mM Tris–HCl buffer, pH 7.4, 1 mM N ‐formyl‐ l ‐kynurenine, 20 μM ZnCl 2 .…”

Section: Methodsmentioning

confidence: 99%

Aerobic tryptophan degradation pathway in bacteria: novel kynurenine formamidase

Kurnasov

Jabloński

Polanuyer

et al. 2003

FEMS Microbiology Letters

113

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While a variety of chemical transformations related to the aerobic degradation of L-tryptophan (kynurenine pathway), and most of the genes and corresponding enzymes involved therein have been predominantly characterized in eukaryotes, relatively little was known about this pathway in bacteria. Using genome comparative analysis techniques we have predicted the existence of the three-step pathway of aerobic L-tryptophan degradation to anthranilate (anthranilate pathway) in several bacteria. Based on the chromosomal gene clustering analysis, we have identified a previously unknown gene encoding for kynurenine formamidase (EC 3.5.1.19) involved with the second step of the anthranilate pathway. This functional prediction was experimentally verified by cloning, expression and enzymatic characterization of recombinant kynurenine formamidase orthologs from Bacillus cereus, Pseudomonas aeruginosa and Ralstonia metallidurans. Experimental verification of the inferred anthranilate pathway was achieved by functional expression in Escherichia coli of the R. metallidurans putative kynBAU operon encoding three required enzymes: tryptophan 2,3-dioxygenase (gene kynA), kynurenine formamidase (gene kynB), and kynureninase (gene kynU). Our data provide the first experimental evidence of the connection between these genes (only one of which, kynU, was previously characterized) and L-tryptophan aerobic degradation pathway in bacteria.

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[29] Arylformamidase from streptomyces parvulus

Cited by 6 publications

References 22 publications

Enzymology of Nad ⁺ Synthesis

Enzymology of Nad ⁺ Synthesis

The Actinomycin Biosynthetic Gene Cluster ofStreptomyces chrysomallus: a Genetic Hall of Mirrors for Synthesis of a Molecule with Mirror Symmetry

Aerobic tryptophan degradation pathway in bacteria: novel kynurenine formamidase

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[29] Arylformamidase from streptomyces parvulus

Cited by 6 publications

References 22 publications

Enzymology of Nad + Synthesis

Enzymology of Nad + Synthesis

The Actinomycin Biosynthetic Gene Cluster ofStreptomyces chrysomallus: a Genetic Hall of Mirrors for Synthesis of a Molecule with Mirror Symmetry

Aerobic tryptophan degradation pathway in bacteria: novel kynurenine formamidase

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Enzymology of Nad ⁺ Synthesis

Enzymology of Nad ⁺ Synthesis