2.3.1.54: formate C-acetyltransferase
This is an abbreviated version!
For detailed information about formate C-acetyltransferase, go to the full flat file.
Word Map on EC 2.3.1.54
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2.3.1.54
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glycyl
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anaerobiosis
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phosphotransacetylase
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chemostats
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homolactic
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glucose-limited
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microaerobic
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pyruvate:ferredoxin
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mixed-acid
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acetoin
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flavodoxins
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activase
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5\'-deoxyadenosyl
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dual-phase
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hypophosphite
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knappe
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benzylsuccinate
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embden-meyerhof-parnas
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biotechnology
-
nutrition
- 2.3.1.54
-
glycyl
- anaerobiosis
- phosphotransacetylase
-
chemostats
-
homolactic
-
glucose-limited
-
microaerobic
-
pyruvate:ferredoxin
-
mixed-acid
- acetoin
- flavodoxins
- activase
-
5\'-deoxyadenosyl
-
dual-phase
- hypophosphite
-
knappe
- benzylsuccinate
-
embden-meyerhof-parnas
- biotechnology
- nutrition
Reaction
Synonyms
AF_1449, formate acetyltransferase, PFL, PFL I, Pfl1, PflB, phosphotransferase system enzyme I, pyruvate formate lyase, pyruvate formate-lyase, pyruvate-formate lyase, pyruvate:formate lyase, pyruvic formate-lyase
ECTree
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Specific Activity
Specific Activity on EC 2.3.1.54 - formate C-acetyltransferase
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additional information
ethanol-producing fermentative metabolism in Chlamydomonas reinhardtii proposed to be initiated by pyruvate formate-lyase, heterologous expression of Chlamydomonas Pfl1 protein in pyruvate formate-lyase-deficient strain of Escherichia coli, enzmye activity under anaerobic conditions regained, Pfl1 fermentation pathway of Chlamydomonas reinhardtii under physiological condition of sulfur depletion analyzed, formate accumulation measured
additional information
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ethanol-producing fermentative metabolism in Chlamydomonas reinhardtii proposed to be initiated by pyruvate formate-lyase, heterologous expression of Chlamydomonas Pfl1 protein in pyruvate formate-lyase-deficient strain of Escherichia coli, enzmye activity under anaerobic conditions regained, Pfl1 fermentation pathway of Chlamydomonas reinhardtii under physiological condition of sulfur depletion analyzed, formate accumulation measured
additional information
mechanistic effect of choosing different protonation states for a substrate carboxylate group that is involved in a salt bridge with an arginine residue analyzed, modeling of arginine-bound carboxylates, computational details, neutral model and anionic model presented, extended model consists of pyruvate in a complex with methylguanidinum and methylthiyl radical, neutral carboxylic acid as a more realistic approximation to the salt bridge arrangement than a bare anionic carboxylate substituent