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Enzymatic reduction of benzoyl‐CoA to alicyclic compounds, a key reaction in anaerobic aromatic metabolism
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| Zeitschriftentitel: | European Journal of Biochemistry |
|---|---|
| Personen und Körperschaften: | , |
| In: | European Journal of Biochemistry, 205, 1992, 1, S. 195-202 |
| Format: | E-Article |
| Sprache: | Englisch |
| veröffentlicht: |
Wiley
|
| Schlagwörter: |
| author_facet |
KOCH, Jürgen FUCHS, Georg KOCH, Jürgen FUCHS, Georg |
|---|---|
| author |
KOCH, Jürgen FUCHS, Georg |
| spellingShingle |
KOCH, Jürgen FUCHS, Georg European Journal of Biochemistry Enzymatic reduction of benzoyl‐CoA to alicyclic compounds, a key reaction in anaerobic aromatic metabolism Biochemistry |
| author_sort |
koch, jürgen |
| spelling |
KOCH, Jürgen FUCHS, Georg 0014-2956 1432-1033 Wiley Biochemistry http://dx.doi.org/10.1111/j.1432-1033.1992.tb16768.x <jats:p>Different anaerobic bacteria can oxidize a variety of aromatic compounds completely to CO<jats:sub>2</jats:sub> via one common aromatic intermediate, benzoyl‐CoA. It has been postulated that anaerobically the aromatic nucleus of benzoyl‐CoA becomes reduced. An oxygen‐sensitive enzyme system is described catalyzing the reduction of benzoyl‐CoA to <jats:italic>trans</jats:italic>‐2‐hydroxycyclohexanecarboxyl‐CoA in a denitrifying <jats:italic>Pseudomonas</jats:italic> species grown anaerobically on benzoate plus nitrate. The assay mixture consists of cell extract, [U‐<jats:sup>14</jats:sup>C]benzoyl‐CoA, a [U‐<jats:sup>14</jats:sup>C]benzoyl‐CoA‐generating system (consisting of [U‐<jats:sup>14</jats:sup>C]benzoate, purified benzoate‐CoA ligase, Mg<jats:sup>2+</jats:sup>‐ATP, coenzyme A), an ATP‐regenerating system (consisting of phospho<jats:italic>enol</jats:italic>pyruvate, pyruvate kinase, myokinase), and a low‐potential reductant [titanium(III) citrate]. The optimal pH is about 7, the specific activity 10 nmol benzoyl‐CoA reduced min<jats:sup>−1</jats:sup>× mg<jats:sup>−1</jats:sup> protein. The apparent <jats:italic>K</jats:italic><jats:sub>m</jats:sub> for benzoyl‐CoA is below 50 μM. Five major products were found. One product is cyclohex‐1‐enecarboxyl‐CoA which must have been formed by a benzoyl‐CoA reductase. The other product is probably <jats:italic>trans</jats:italic>‐2‐hydroxycyclohexanecarboxyl‐CoA rather than the <jats:italic>cis</jats:italic>‐stereoisomer; this product must have been formed by a cyclohex‐1‐enecarboxyl‐CoA hydratase. Two other products are likely to be intermediates of benzoyl‐CoA reduction to cyclohex‐1‐enecarboxyl‐CoA, suggesting that the reduction reaction is more complex. An early formed fifth product is more polar than cyclohexanecarboxyl‐ or cyclohex‐1‐enecarboxyl‐CoA.</jats:p><jats:p>The enzyme system is under oxygen control since it was not found in cells grown aerobically on benzoate. It is induced by aromatic compounds since its activity is low in cells grown anaerobically on acetate. The actual inducer is probably benzoyl‐CoA rather than benzoate. This conclusion is drawn from the fact that the system is also present in cells grown anaerobically on phenol, phenylacetate, 4‐hydroxybenzoate, or 2‐aminobenzoate; the anaerobic metabolism of these compounds has been shown in this organism to proceed directly via benzoyl‐CoA rather than via free benzoate.</jats:p> Enzymatic reduction of benzoyl‐CoA to alicyclic compounds, a key reaction in anaerobic aromatic metabolism European Journal of Biochemistry |
| doi_str_mv |
10.1111/j.1432-1033.1992.tb16768.x |
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Online Free |
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Chemie und Pharmazie |
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ElectronicArticle |
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Wiley, 1992 |
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Wiley, 1992 |
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0014-2956 1432-1033 |
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0014-2956 1432-1033 |
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English |
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koch1992enzymaticreductionofbenzoylcoatoalicycliccompoundsakeyreactioninanaerobicaromaticmetabolism |
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1992 |
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Wiley |
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ai |
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ai |
| series |
European Journal of Biochemistry |
| source_id |
49 |
| title |
Enzymatic reduction of benzoyl‐CoA to alicyclic compounds, a key reaction in anaerobic aromatic metabolism |
| title_unstemmed |
Enzymatic reduction of benzoyl‐CoA to alicyclic compounds, a key reaction in anaerobic aromatic metabolism |
| title_full |
Enzymatic reduction of benzoyl‐CoA to alicyclic compounds, a key reaction in anaerobic aromatic metabolism |
| title_fullStr |
Enzymatic reduction of benzoyl‐CoA to alicyclic compounds, a key reaction in anaerobic aromatic metabolism |
| title_full_unstemmed |
Enzymatic reduction of benzoyl‐CoA to alicyclic compounds, a key reaction in anaerobic aromatic metabolism |
| title_short |
Enzymatic reduction of benzoyl‐CoA to alicyclic compounds, a key reaction in anaerobic aromatic metabolism |
| title_sort |
enzymatic reduction of benzoyl‐coa to alicyclic compounds, a key reaction in anaerobic aromatic metabolism |
| topic |
Biochemistry |
| url |
http://dx.doi.org/10.1111/j.1432-1033.1992.tb16768.x |
| publishDate |
1992 |
| physical |
195-202 |
| description |
<jats:p>Different anaerobic bacteria can oxidize a variety of aromatic compounds completely to CO<jats:sub>2</jats:sub> via one common aromatic intermediate, benzoyl‐CoA. It has been postulated that anaerobically the aromatic nucleus of benzoyl‐CoA becomes reduced. An oxygen‐sensitive enzyme system is described catalyzing the reduction of benzoyl‐CoA to <jats:italic>trans</jats:italic>‐2‐hydroxycyclohexanecarboxyl‐CoA in a denitrifying <jats:italic>Pseudomonas</jats:italic> species grown anaerobically on benzoate plus nitrate. The assay mixture consists of cell extract, [U‐<jats:sup>14</jats:sup>C]benzoyl‐CoA, a [U‐<jats:sup>14</jats:sup>C]benzoyl‐CoA‐generating system (consisting of [U‐<jats:sup>14</jats:sup>C]benzoate, purified benzoate‐CoA ligase, Mg<jats:sup>2+</jats:sup>‐ATP, coenzyme A), an ATP‐regenerating system (consisting of phospho<jats:italic>enol</jats:italic>pyruvate, pyruvate kinase, myokinase), and a low‐potential reductant [titanium(III) citrate]. The optimal pH is about 7, the specific activity 10 nmol benzoyl‐CoA reduced min<jats:sup>−1</jats:sup>× mg<jats:sup>−1</jats:sup> protein. The apparent <jats:italic>K</jats:italic><jats:sub>m</jats:sub> for benzoyl‐CoA is below 50 μM. Five major products were found. One product is cyclohex‐1‐enecarboxyl‐CoA which must have been formed by a benzoyl‐CoA reductase. The other product is probably <jats:italic>trans</jats:italic>‐2‐hydroxycyclohexanecarboxyl‐CoA rather than the <jats:italic>cis</jats:italic>‐stereoisomer; this product must have been formed by a cyclohex‐1‐enecarboxyl‐CoA hydratase. Two other products are likely to be intermediates of benzoyl‐CoA reduction to cyclohex‐1‐enecarboxyl‐CoA, suggesting that the reduction reaction is more complex. An early formed fifth product is more polar than cyclohexanecarboxyl‐ or cyclohex‐1‐enecarboxyl‐CoA.</jats:p><jats:p>The enzyme system is under oxygen control since it was not found in cells grown aerobically on benzoate. It is induced by aromatic compounds since its activity is low in cells grown anaerobically on acetate. The actual inducer is probably benzoyl‐CoA rather than benzoate. This conclusion is drawn from the fact that the system is also present in cells grown anaerobically on phenol, phenylacetate, 4‐hydroxybenzoate, or 2‐aminobenzoate; the anaerobic metabolism of these compounds has been shown in this organism to proceed directly via benzoyl‐CoA rather than via free benzoate.</jats:p> |
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| author | KOCH, Jürgen, FUCHS, Georg |
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| description | <jats:p>Different anaerobic bacteria can oxidize a variety of aromatic compounds completely to CO<jats:sub>2</jats:sub> via one common aromatic intermediate, benzoyl‐CoA. It has been postulated that anaerobically the aromatic nucleus of benzoyl‐CoA becomes reduced. An oxygen‐sensitive enzyme system is described catalyzing the reduction of benzoyl‐CoA to <jats:italic>trans</jats:italic>‐2‐hydroxycyclohexanecarboxyl‐CoA in a denitrifying <jats:italic>Pseudomonas</jats:italic> species grown anaerobically on benzoate plus nitrate. The assay mixture consists of cell extract, [U‐<jats:sup>14</jats:sup>C]benzoyl‐CoA, a [U‐<jats:sup>14</jats:sup>C]benzoyl‐CoA‐generating system (consisting of [U‐<jats:sup>14</jats:sup>C]benzoate, purified benzoate‐CoA ligase, Mg<jats:sup>2+</jats:sup>‐ATP, coenzyme A), an ATP‐regenerating system (consisting of phospho<jats:italic>enol</jats:italic>pyruvate, pyruvate kinase, myokinase), and a low‐potential reductant [titanium(III) citrate]. The optimal pH is about 7, the specific activity 10 nmol benzoyl‐CoA reduced min<jats:sup>−1</jats:sup>× mg<jats:sup>−1</jats:sup> protein. The apparent <jats:italic>K</jats:italic><jats:sub>m</jats:sub> for benzoyl‐CoA is below 50 μM. Five major products were found. One product is cyclohex‐1‐enecarboxyl‐CoA which must have been formed by a benzoyl‐CoA reductase. The other product is probably <jats:italic>trans</jats:italic>‐2‐hydroxycyclohexanecarboxyl‐CoA rather than the <jats:italic>cis</jats:italic>‐stereoisomer; this product must have been formed by a cyclohex‐1‐enecarboxyl‐CoA hydratase. Two other products are likely to be intermediates of benzoyl‐CoA reduction to cyclohex‐1‐enecarboxyl‐CoA, suggesting that the reduction reaction is more complex. An early formed fifth product is more polar than cyclohexanecarboxyl‐ or cyclohex‐1‐enecarboxyl‐CoA.</jats:p><jats:p>The enzyme system is under oxygen control since it was not found in cells grown aerobically on benzoate. It is induced by aromatic compounds since its activity is low in cells grown anaerobically on acetate. The actual inducer is probably benzoyl‐CoA rather than benzoate. This conclusion is drawn from the fact that the system is also present in cells grown anaerobically on phenol, phenylacetate, 4‐hydroxybenzoate, or 2‐aminobenzoate; the anaerobic metabolism of these compounds has been shown in this organism to proceed directly via benzoyl‐CoA rather than via free benzoate.</jats:p> |
| doi_str_mv | 10.1111/j.1432-1033.1992.tb16768.x |
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| id | ai-49-aHR0cDovL2R4LmRvaS5vcmcvMTAuMTExMS9qLjE0MzItMTAzMy4xOTkyLnRiMTY3NjgueA |
| imprint | Wiley, 1992 |
| imprint_str_mv | Wiley, 1992 |
| institution | DE-Bn3, DE-Brt1, DE-Zwi2, DE-D161, DE-Zi4, DE-Gla1, DE-15, DE-Pl11, DE-Rs1, DE-14, DE-105, DE-Ch1, DE-L229, DE-D275 |
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| match_str | koch1992enzymaticreductionofbenzoylcoatoalicycliccompoundsakeyreactioninanaerobicaromaticmetabolism |
| mega_collection | Wiley (CrossRef) |
| physical | 195-202 |
| publishDate | 1992 |
| publishDateSort | 1992 |
| publisher | Wiley |
| record_format | ai |
| recordtype | ai |
| series | European Journal of Biochemistry |
| source_id | 49 |
| spelling | KOCH, Jürgen FUCHS, Georg 0014-2956 1432-1033 Wiley Biochemistry http://dx.doi.org/10.1111/j.1432-1033.1992.tb16768.x <jats:p>Different anaerobic bacteria can oxidize a variety of aromatic compounds completely to CO<jats:sub>2</jats:sub> via one common aromatic intermediate, benzoyl‐CoA. It has been postulated that anaerobically the aromatic nucleus of benzoyl‐CoA becomes reduced. An oxygen‐sensitive enzyme system is described catalyzing the reduction of benzoyl‐CoA to <jats:italic>trans</jats:italic>‐2‐hydroxycyclohexanecarboxyl‐CoA in a denitrifying <jats:italic>Pseudomonas</jats:italic> species grown anaerobically on benzoate plus nitrate. The assay mixture consists of cell extract, [U‐<jats:sup>14</jats:sup>C]benzoyl‐CoA, a [U‐<jats:sup>14</jats:sup>C]benzoyl‐CoA‐generating system (consisting of [U‐<jats:sup>14</jats:sup>C]benzoate, purified benzoate‐CoA ligase, Mg<jats:sup>2+</jats:sup>‐ATP, coenzyme A), an ATP‐regenerating system (consisting of phospho<jats:italic>enol</jats:italic>pyruvate, pyruvate kinase, myokinase), and a low‐potential reductant [titanium(III) citrate]. The optimal pH is about 7, the specific activity 10 nmol benzoyl‐CoA reduced min<jats:sup>−1</jats:sup>× mg<jats:sup>−1</jats:sup> protein. The apparent <jats:italic>K</jats:italic><jats:sub>m</jats:sub> for benzoyl‐CoA is below 50 μM. Five major products were found. One product is cyclohex‐1‐enecarboxyl‐CoA which must have been formed by a benzoyl‐CoA reductase. The other product is probably <jats:italic>trans</jats:italic>‐2‐hydroxycyclohexanecarboxyl‐CoA rather than the <jats:italic>cis</jats:italic>‐stereoisomer; this product must have been formed by a cyclohex‐1‐enecarboxyl‐CoA hydratase. Two other products are likely to be intermediates of benzoyl‐CoA reduction to cyclohex‐1‐enecarboxyl‐CoA, suggesting that the reduction reaction is more complex. An early formed fifth product is more polar than cyclohexanecarboxyl‐ or cyclohex‐1‐enecarboxyl‐CoA.</jats:p><jats:p>The enzyme system is under oxygen control since it was not found in cells grown aerobically on benzoate. It is induced by aromatic compounds since its activity is low in cells grown anaerobically on acetate. The actual inducer is probably benzoyl‐CoA rather than benzoate. This conclusion is drawn from the fact that the system is also present in cells grown anaerobically on phenol, phenylacetate, 4‐hydroxybenzoate, or 2‐aminobenzoate; the anaerobic metabolism of these compounds has been shown in this organism to proceed directly via benzoyl‐CoA rather than via free benzoate.</jats:p> Enzymatic reduction of benzoyl‐CoA to alicyclic compounds, a key reaction in anaerobic aromatic metabolism European Journal of Biochemistry |
| spellingShingle | KOCH, Jürgen, FUCHS, Georg, European Journal of Biochemistry, Enzymatic reduction of benzoyl‐CoA to alicyclic compounds, a key reaction in anaerobic aromatic metabolism, Biochemistry |
| title | Enzymatic reduction of benzoyl‐CoA to alicyclic compounds, a key reaction in anaerobic aromatic metabolism |
| title_full | Enzymatic reduction of benzoyl‐CoA to alicyclic compounds, a key reaction in anaerobic aromatic metabolism |
| title_fullStr | Enzymatic reduction of benzoyl‐CoA to alicyclic compounds, a key reaction in anaerobic aromatic metabolism |
| title_full_unstemmed | Enzymatic reduction of benzoyl‐CoA to alicyclic compounds, a key reaction in anaerobic aromatic metabolism |
| title_short | Enzymatic reduction of benzoyl‐CoA to alicyclic compounds, a key reaction in anaerobic aromatic metabolism |
| title_sort | enzymatic reduction of benzoyl‐coa to alicyclic compounds, a key reaction in anaerobic aromatic metabolism |
| title_unstemmed | Enzymatic reduction of benzoyl‐CoA to alicyclic compounds, a key reaction in anaerobic aromatic metabolism |
| topic | Biochemistry |
| url | http://dx.doi.org/10.1111/j.1432-1033.1992.tb16768.x |