Purification and characterization of rice α-glucosidase, a key enzyme for alcohol fermentation of rice polish

2003 ◽  
Vol 95 (1) ◽  
pp. 106-108 ◽  
Author(s):  
Hiroshi Iwata ◽  
Toshiaki Suzuki ◽  
Isao Aramaki
Keyword(s):  
Purification And Characterization ◽  
Alcohol Fermentation ◽  
Key Enzyme

scholarly journals Purification and characterization of eucaryotic alanine racemase acting as key enzyme in cyclosporin biosynthesis.

1994 ◽  
Vol 269 (17) ◽  
pp. 12710-12714
Author(s):  
K. Hoffmann ◽  
E. Schneider-Scherzer ◽  
H. Kleinkauf ◽  
R. Zocher
Keyword(s):  
Alanine Racemase ◽  
Purification And Characterization ◽  
Key Enzyme

scholarly journals Purification and Characterization of the Endoglycosidase Heparanase 1 from Human Plantar Stratum Corneum: a Key Enzyme in Epidermal Physiology?

2001 ◽  
Vol 117 (5) ◽  
pp. 1266-1273 ◽  
Author(s):  
Dominique Bernard ◽  
Bruno Méhul ◽  
Caroline Delattre ◽  
Lucie Simonetti ◽  
Agnès Thomas-Collignon ◽  
...  
Keyword(s):  
Stratum Corneum ◽  
Purification And Characterization ◽  
Key Enzyme ◽  
Plantar Stratum Corneum

Purification and characterization of 1-SST, the key enzyme initiating fructan biosynthesis in young chicory roots (Cichorium intybus)

1996 ◽  
Vol 98 (3) ◽  
pp. 455-466 ◽  
Author(s):  
Wim Ende ◽  
Dominik Wonterghem ◽  
Erna Dewil ◽  
Peter Verhaert ◽  
Arnold Loof ◽  
...  
Keyword(s):  
Cichorium Intybus ◽  
Purification And Characterization ◽  
Key Enzyme ◽  
Chicory Roots

scholarly journals Purification and Characterization of (Per)Chlorate Reductase from the Chlorate-Respiring Strain GR-1

1999 ◽  
Vol 181 (21) ◽  
pp. 6706-6711 ◽  
Author(s):  
Servé W. M. Kengen ◽  
Geoffrey B. Rikken ◽  
Wilfred R. Hagen ◽  
Cees G. van Ginkel ◽  
Alfons J. M. Stams
Keyword(s):  
Electron Paramagnetic Resonance Spectroscopy ◽  
Bacterial Species ◽  
Intermediate Formation ◽  
Resonance Spectroscopy ◽  
Purification And Characterization ◽  
Paramagnetic Resonance ◽  
Terminal Electron Acceptor ◽  
Key Enzyme ◽  
Chlorate Reductase

ABSTRACT Strain GR-1 is one of several recently isolated bacterial species that are able to respire by using chlorate or perchlorate as the terminal electron acceptor. The organism performs a complete reduction of chlorate or perchlorate to chloride and oxygen, with the intermediate formation of chlorite. This study describes the purification and characterization of the key enzyme of the reductive pathway, the chlorate and perchlorate reductase. A single enzyme was found to catalyze both the chlorate- and perchlorate-reducing activity. The oxygen-sensitive enzyme was located in the periplasm and had an apparent molecular mass of 420 kDa, with subunits of 95 and 40 kDa in an α3β3 composition. Metal analysis showed the presence of 11 mol of iron, 1 mol of molybdenum, and 1 mol of selenium per mol of heterodimer. In accordance, quantitative electron paramagnetic resonance spectroscopy showed the presence of one [3Fe-4S] cluster and two [4Fe-4S] clusters. Furthermore, two different signals were ascribed to Mo(V). The Km values for perchlorate and chlorate were 27 and <5 μM, respectively. Besides perchlorate and chlorate, nitrate, iodate, and bromate were also reduced at considerable rates. The resemblance of the enzyme to nitrate reductases, formate dehydrogenases, and selenate reductase is discussed.

scholarly journals Biodegradation of phenanthrene by Pseudomonas sp. strain PPD: purification and characterization of 1-hydroxy-2-naphthoic acid dioxygenase

Microbiology ◽  
2009 ◽  
Vol 155 (9) ◽  
pp. 3083-3091 ◽  
Author(s):  
Jaigeeth Deveryshetty ◽  
Prashant S. Phale
Keyword(s):  
Molecular Mass ◽  
Substrate Inhibition ◽  
Enzyme Reaction ◽  
Sole Source ◽  
Purification And Characterization ◽  
Spectral Changes ◽  
Native Molecular Mass ◽  
Naphthoic Acid ◽  
Key Enzyme

Pseudomonas sp. strain PPD can metabolize phenanthrene as the sole source of carbon and energy via the ‘phthalic acid’ route. The key enzyme, 1-hydroxy-2-naphthoic acid dioxygenase (1-HNDO, EC 1.13.11.38), was purified to homogeneity using a 3-hydroxy-2-naphthoic acid (3-H2NA)-affinity matrix. The enzyme was a homotetramer with a native molecular mass of 160 kDa and subunit molecular mass of ∼39 kDa. It required Fe(II) as the cofactor and was specific for 1-hydroxy-2-naphthoic acid (1-H2NA), with K m 13.5 μM and V max 114 μmol min−1 mg−1. 1-HNDO failed to show activity with gentisic acid, salicylic acid and other hydroxynaphthoic acids tested. Interestingly, the enzyme showed substrate inhibition with a K i of 116 μM. 1-HNDO was found to be competitively inhibited by 3-H2NA with a K i of 24 μM. Based on the pH-dependent spectral changes, the enzyme reaction product was identified as 2-carboxybenzalpyruvic acid. Under anaerobic conditions, the enzyme failed to convert 1-H2NA to 2-carboxybenzalpyruvic acid. Stoichiometric studies showed the incorporation of 1 mol O2 into the substrate to yield 1 mol product. These results suggest that 1-HNDO from Pseudomonas sp. strain PPD is an extradiol-type ring-cleaving dioxygenase.

Purification and characterization of 1-SST, the key enzyme initiating fructan biosynthesis in young chicory roots (Cichorium intybus)

1996 ◽  
Vol 98 (3) ◽  
pp. 455-466 ◽  
Author(s):  
Wim Van den Ende ◽  
Dominik Van Wonterghem ◽  
Erna Dewil ◽  
Peter Verhaert ◽  
Arnold De Loof ◽  
...  
Keyword(s):  
Cichorium Intybus ◽  
Purification And Characterization ◽  
Key Enzyme ◽  
Chicory Roots

scholarly journals Purification and Characterization of the Acetone Carboxylase of Cupriavidus metallidurans Strain CH34

2012 ◽  
Vol 78 (12) ◽  
pp. 4516-4518 ◽  
Author(s):  
Caroline Rosier ◽  
Natalie Leys ◽  
Céline Henoumont ◽  
Max Mergeay ◽  
Ruddy Wattiez
Keyword(s):  
Purification And Characterization ◽  
Content Type ◽  
Cupriavidus Metallidurans ◽  
Key Enzyme ◽  
Genome Analyses

ABSTRACTAcetone carboxylase (Acx) is a key enzyme involved in the biodegradation of acetone by bacteria. Except for theHelicobacteraceaefamily, genome analyses revealed that bacteria that possess an Acx, such asCupriavidus metalliduransstrain CH34, are associated with soil. The Acx of CH34 forms the heterohexameric complex α2β2γ2and can carboxylate only acetone and 2-butanone in an ATP-dependent reaction to acetoacetate and 3-keto-2-methylbutyrate, respectively.

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