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Microbial transformation of pyridine compounds

O P Shukla
- Vol. 93, Iss: 7, pp 1143-1153
TLDR
Biodegradation of isoniazid and isonicotinate appears to be more complex and formation of characteristic pigments suggests the involvement of hydroxylated compounds as intermediates.
Abstract
Studies on biotransformation of pyridine derivatives have revealed two alternative patterns of biodegradation. Pyridine and α-picoline are not degradedvia the hydroxylated derivatives. A reductive pathway involving succinic semialdehyde (SSA) or glutaric semialdehyde is involved in degradation of pyridine, α-picoline and possibly other alkyl pyridines. α-Picolinate, nicotinate, isonicotinate and hydroxypyridines are degradedvia hydroxypyridine derivatives. Studies on aNocardia strain capable of growth on pyridine-N-oxide (PNO), 2-hydroxypyridine and pyridine rule out the involvement of PNO or 2-hydroxypyridine in pyridine metabolism. PNO is metabolizedvia 2-hydroxypyridine while pyridine is metabolizedvia SSA. Biodegradation of isoniazid and isonicotinate (INA) appears to be more complex. INA is degraded in several organismsvia 2-hydroxy INA and citrazinic acid. However, a strain ofBacillus brevis isolated in our, laboratory metabolises isonicotinatevia SSA, and a pathway similar to that of N-methyl-INA may be operative. Several organisms degrading quinoline and isoquinoline have been isolated. Formation of characteristic pigments suggests the involvement of hydroxylated compounds as intermediates.

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Journal ArticleDOI

Microbial transformation of azaarenes and potential uses in pharmaceutical synthesis.

TL;DR: Pyridine, quinoline, acridine, indole, carbazole, and other heterocyclic nitrogen-containing compounds (azaarenes) can be transformed by cultures of bacteria and fungi to produce a variety of new derivatives, many of which have biological activity.
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A 2-Hydroxypyridine Catabolism Pathway in Rhodococcus rhodochrous Strain PY11.

TL;DR: It is reported that in Rhodococcus rhodochrous PY11, the initial hydroxylation of 2-hydroxypyridine is catalyzed by a four-component dioxygenase (HpoBCDF), and it is shown that the subsequent 2,3,6-trihydroxYPyridine ring opening is catalyzing by the hypothetical cyclase HpoH.
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Novel regioselective hydroxylations of pyridine carboxylic acids at position C2 and pyrazine carboxylic acids at position C3.

TL;DR: It is shown that the enzymatic activity of 6-methylnicotinate-2-oxidoreductase can be used for the preparation of a series of hydroxylated heterocyclic carboxylic acid derivatives, and is so far the only known strain which allows the microbial production of both these compounds and 3-hydroxypyrazine- 2-carboxy Lic acid and3-hydroxy-5-chloroypyrazine
Journal ArticleDOI

Isolation of new 6-methylnicotinic-acid-degrading bacteria, one of which catalyses the regioselective hydroxylation of nicotinic acid at position C2

TL;DR: Evidence is presented that the first step in the degradation pathway of strain Mena 23/3–3c is hydroxylation at the C2 position, and evidence that the highest degree of 16S rRNA sequence similarity to members of the genera Ralstonia and Burkholderia is presented.
Journal ArticleDOI

3-Hydroxypyridine Dehydrogenase HpdA Is Encoded by a Novel Four-Component Gene Cluster and Catalyzes the First Step of 3-Hydroxypyridine Catabolism in Ensifer adhaerens HP1.

TL;DR: The results demonstrated that the PEP-utilizing protein and pyruvate-phosphate dikinase were involved in the HpdA activity, and the presence of the gene cluster 3hpd was discovered in the genomes of diverse microbial strains.
References
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Journal ArticleDOI

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Journal ArticleDOI

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TL;DR: N-Formylmaleamic acid, a probable intermediate in the bacterial metabolism of nicotinic acid, has been synthesized by photoisomerization of its transisomer, N-formylfumaramic acid.
Journal ArticleDOI

Microbial metabolism of the pyridine ring. Metabolic pathways of pyridine biodegradation by soil bacteria.

TL;DR: Cell-free extracts were unable to metabolize pyridine even after supplementation with a variety of cofactors or protecting agents and two mutants of this bacillus, selected for their inability to grow on pyrsidine were deficient in succinate semialdehyde dehydrogenase.
Journal ArticleDOI

The Pathway of Nicotinic Acid Oxidation by a Bacillus Species

TL;DR: A different pathway of nicotinic acid oxidation utilized by a Bacillus species isolated from soil is described, which involves hydrolytic deamination to maleic acid, which is then isomerized to fumaric acid.
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