scholarly journals Mechanistic and Structural Insight to an Evolved Benzoylformate Decarboxylase with Enhanced Pyruvate Decarboxylase Activity

Catalysts ◽  
2016 ◽  
Vol 6 (12) ◽  
pp. 190 ◽  
Author(s):  
Forest Andrews ◽  
Cindy Wechsler ◽  
Megan Rogers ◽  
Danilo Meyer ◽  
Kai Tittmann ◽  
...  
Keyword(s):  
Pyruvate Decarboxylase ◽  
Decarboxylase Activity ◽  
Benzoylformate Decarboxylase ◽  
Structural Insight

scholarly journals Pyruvate decarboxylase activity is regulated by the Ser/Thr protein phosphatase Sit4p in the yeastSaccharomyces cerevisiae

2013 ◽  
Vol 13 (6) ◽  
pp. 518-528 ◽  
Author(s):  
Leandro José de Assis ◽  
Russolina Benedeta Zingali ◽  
Claudio Akio Masuda ◽  
Silas Pessini Rodrigues ◽  
Monica Montero-Lomelí
Keyword(s):  
Protein Phosphatase ◽  
Pyruvate Decarboxylase ◽  
Decarboxylase Activity

A New Test for the Determination of Pyruvate Decarboxylase Activity

1968 ◽  
Vol 7 (11) ◽  
pp. 886-887 ◽  
Author(s):  
A. Schellenberger ◽  
G. Hübner ◽  
H. Lehmann
Keyword(s):  
Pyruvate Decarboxylase ◽  
Decarboxylase Activity

scholarly journals Pyruvate decarboxylase in minimally processed young palm cladode

2020 ◽  
Vol 9 (7) ◽  
pp. e340973755
Author(s):  
Larissa Félix Macêdo ◽  
Franciscleudo Bezerra da Costa ◽  
Ana Marinho do Nascimento ◽  
Jéssica Leite da Silva ◽  
Osvaldo Soares da Silva ◽  
...  
Keyword(s):  
Soluble Sugars ◽  
Pyruvate Decarboxylase ◽  
Titratable Acidity ◽  
Soluble Solids ◽  
Decarboxylase Activity ◽  
Total Chlorophyll ◽  
Minimally Processed ◽  
Total Carotenoids ◽  
Analysis Center

The palm is a cactaceous of great global importance, being the young cladodes minimally processed a viable alternative consumption for cooking. Among the studied palm variables, enzymes play a major role in the post-harvest quality of these species, generating oxidation and influencing the sensory attributes of cladodes. Therefore, the objective was to estimate the pyruvate decarboxylase activity in young cladodes of 'Tiny' palms - Nopalea cochenilifera and 'Ear Mexican Elephant' - Opuntia tuna minimally processed. The experiment was conducted in the Laboratory of Chemistry, Biochemistry and Food Analysis Center of Science and Technology Agrifood the Federal University of Campina Grande, Campus Pombal, Paraíba. The young cladodes were minimally processed and the analyzes were performed immediately after processing, with 24 and 48 hours of incubation under controlled temperature (22 ± 2°C). The analyzes performed were activity of the enzyme pyruvate decarboxylase (PDC), pH, soluble solids, titratable acidity, ratio, soluble sugars, total chlorophyll, total carotenoids, ascorbic acid and phenolic compounds. There was enzymatic activity of pyruvate decarboxylase from young minimally processed cladodes for the species studied, with greater activity in the cladodes of the species 'Tiny'.

scholarly journals Reduction of The Pyruvate Decarboxylase Activity Improves Isobutanol Production By Klebsiella Pneumoniae

2021 ◽  
Author(s):  
Lin Shu ◽  
Jinjie Gu ◽  
Qinghui Wang ◽  
Shaoqi Sun ◽  
Youtian Cui ◽  
...  
Keyword(s):  
Klebsiella Pneumoniae ◽  
Single Point ◽  
Pyruvate Decarboxylase ◽  
Catalytic Efficiency ◽  
Decarboxylase Activity ◽  
Enzymatic Reactions ◽  
Substrate Conversion ◽  
High Level

Abstract Background Klebsiella pneumoniae contains an endogenous isobutanol synthesis pathway. ipdC, annotated as an indole-3-pyruvate decarboxylase (Kp-IpdC), was identified to catalyze the formation of isobutyraldehyde from 2-ketoisovalerate. Results Compared with 2-ketoisovalerate decarboxylase from Lactococcus lactis (KivD), a decarboxylase commonly used in artificial isobutanol synthesis, Kp-IpdC has an 2.8-fold lower Km for 2-ketoisovalerate, leading to higher isobutanol production without induction. However, high level expression of ipdC by induction resulted in a low isobutanol titer. In vitro enzymatic reactions showed that Kp-IpdC exhibits promiscuous pyruvate decarboxylase activity, which adversely consume the available pyruvate precursor for isobutanol synthesis. To address this we have engineered Kp-IpdC to reduce pyruvate decarboxylase activity. From computational modeling we identified 10 residues surrounding the active site for mutagenesis. Ten designs consisting of eight single-point mutants and two double-mutants were selected for exploration. Mutants L546W and T290L showed 5.1% and 22.1% of catalytic efficiency on pyruvate, which were then expressed in K. pneumoniae for in vivo test. Isobutanol production by K. pneumoniae T290L was 25% higher than the control strain, and a final titer of 5.5 g/L isobutanol was obtained with a substrate conversion ratio of 0.16 mol/mol glucose. Conclusions This research provides a new way to improve the efficiency of the biological route of isobutanol production.

scholarly journals Acetaldehyde formation by mitochondria from the free-living nematode Panagrellus redivivus

1984 ◽  
Vol 221 (2) ◽  
pp. 535-540 ◽  
Author(s):  
J Barrett ◽  
P E Butterworth
Keyword(s):  
Pyruvate Dehydrogenase Complex ◽  
Pyruvate Decarboxylase ◽  
Thiol Group ◽  
Mitochondrial Fraction ◽  
Decarboxylase Activity ◽  
Free Living ◽  
Panagrellus Redivivus ◽  
Free Living Nematode ◽  
Acetaldehyde Production ◽  
Thiamin Pyrophosphate

The mitochondrial fraction from the free-living nematode Panagrellus redivivus decarboxylates pyruvate to produce significant amounts of acetaldehyde. Acetaldehyde formation is stimulated by thiamin pyrophosphate, shows a sharp optimum at pH 6.8 and is greater under anaerobic than aerobic conditions. The pyruvate decarboxylase activity cofractionates with, and is probably a partial reaction of, the pyruvate dehydrogenase complex. Acetaldehyde production is modulated by NAD+, ATP and acetyl-CoA and is greatly stimulated by lipoic acid. The pyruvate decarboxylase system is extremely sensitive to thiol-group inhibitors and is inhibited by oxygen in the presence of pyruvate.

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