4.1.1.74: indolepyruvate decarboxylase
This is an abbreviated version!
For detailed information about indolepyruvate decarboxylase, go to the full flat file.
Word Map on EC 4.1.1.74
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4.1.1.74
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iaa
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azospirillum
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cloacae
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enterobacter
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brasilense
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growth-promoting
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decarboxylases
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indole-3-acetaldehyde
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l-tryptophan
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zymomonas
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tryptophol
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mobilis
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2-keto
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benzoylformate
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phenylpyruvate
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diphosphate-dependent
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synthesis
- 4.1.1.74
- iaa
- azospirillum
- cloacae
- enterobacter
- brasilense
-
growth-promoting
- decarboxylases
- indole-3-acetaldehyde
- l-tryptophan
-
zymomonas
- tryptophol
- mobilis
-
2-keto
- benzoylformate
- phenylpyruvate
-
diphosphate-dependent
- synthesis
Reaction
Synonyms
Decarboxylase, indolepyruvate, Decarboxylase, indolepyruvate (Enterobacter agglomerans clone pMB2 gene ipdC reduced), GenBank L80006-derived protein GI 1507711, Indole-3-pyruvate decarboxylase, indole-3-pyruvic acid decarboxylase, Indolepyruvate decarboxylase, Indolepyruvate decarboxylase (Enterobacter herbocola strain 299R clone pMB2 gene ipdC reduced), Indolepyruvic acid decarboxylase, IpdC, Ipyr, IPyr decarboxylase, KivD
ECTree
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Application
Application on EC 4.1.1.74 - indolepyruvate decarboxylase
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synthesis
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engineering of a strain of Corynebacterium glutamicum, based on inactivation of the pyruvate dehydrogenase complex, pyruvate:quinone oxidoreductase, transaminase B, and additional overexpression of the ilvBNCD genes, encoding acetohydroxyacid synthase, acetohydroxyacid isomeroreductase, and dihydroxyacid dehydratase, for the production of isobutanol from glucose under oxygen deprivation conditions by inactivation of L-lactate and malate dehydrogenases, implementation of ketoacid decarboxylase from Lactococcus lactis, alcohol dehydrogenase 2 (ADH2) from Saccharomyces cerevisiae, and expression of the pntAB transhydrogenase genes from Escherichia coli. The resulting strain produces isobutanol with a substrate-specific yield (YP/S) of 0.60 mol per mol of glucose. Chromosomally encoded alcohol dehydrogenase AdhA rather than the plasmid-encoded ADH2 from S. cerevisiae is involved in isobutanol formation, and overexpression of the corresponding AdhA gene increases the YP/S to 0.77 mol of isobutanol per mol of glucose. Inactivation of the malic enzyme significantly reduces the YP/S, indicating that the metabolic cycle consisting of pyruvate and/or phosphoenolpyruvate carboxylase, malate dehydrogenase, and malic enzyme is responsible for the conversion of NADH + H+ to NADPH + H+. In fed-batch fermentations with an aerobic growth phase and an oxygen-depleted production phase, the most promising strain produces about 175 mM isobutanol, with a volumetric productivity of 4.4 mM per h, and shows an overall YP/S of about 0.48 mol per mol of glucose in the production phase
synthesis
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engineering of Clostridium thermocellum to produce isobutanol. Both the native 2-oxoisovalerate-oxidoreductase KOR, EC 1.2.7.7, and the heterologous Lactococcus lactis 2-oxoisovalerate decarboxylase KIVD, EC 4.1.1.74, expressed are responsible for isobutanol production.The plasmid is integrated into the chromosome by single crossover. The resulting strain is stable without antibiotic selection pressure and produces 5.4g/l of isobutanol from cellulose in minimal medium at 50°C within 75 h, corresponding to 41% of theoretical yield