scholarly journals Crystallization of Membrane-bound Alcohol Dehydrogenase of Acetic Acid Bacteria

1982 ◽  
Vol 46 (11) ◽  
pp. 2859-2863
Author(s):  
Osao Adachi ◽  
Emiko Shinagawa ◽  
Kazunobu Matsushita ◽  
Minoru Ameyama
Keyword(s):  
Acetic Acid ◽  
Alcohol Dehydrogenase ◽  
Acetic Acid Bacteria ◽  
Membrane Bound

scholarly journals Membrane-bound Sugar Alcohol Dehydrogenase in Acetic Acid Bacteria catalyzes L-Ribulose Formation and NAD-Dependent Ribitol Dehydrogenase is Independent of the Oxidative Fermentation

2001 ◽  
Vol 65 (1) ◽  
pp. 115-125 ◽  
Author(s):  
Osao ADACHI ◽  
Yoshikazu FUJII ◽  
Yoshitaka ANO ◽  
Duangtip MOONMANGMEE ◽  
Hirohide TOYAMA ◽  
...  
Keyword(s):  
Acetic Acid ◽  
Alcohol Dehydrogenase ◽  
Acetic Acid Bacteria ◽  
Sugar Alcohol ◽  
Membrane Bound ◽  
Ribitol Dehydrogenase

scholarly journals The inactive and active forms of the pyrroloquinoline quinone-alcohol dehydrogenase of Gluconacetobacter diazotrophicus: a comparative study

2013 ◽  
Vol 2 (1s) ◽  
pp. 2 ◽  
Author(s):  
Saul Gomez-Manzo ◽  
Irene Patricia Del Arenal-Mena ◽  
Edgardo Escamilla
Keyword(s):  
Acetic Acid ◽  
Alcohol Dehydrogenase ◽  
Comparative Study ◽  
Redox State ◽  
Catalytic Properties ◽  
Acetic Acid Bacteria ◽  
Pyrroloquinoline Quinone ◽  
Gluconacetobacter Diazotrophicus ◽  
Membrane Bound ◽  
Prosthetic Groups

<em>Gluconacetobacter diazotrophicus</em> as a member of the acetic acid bacteria group, oxidize alcohol to acetic acid through two sequential reactions catalyzed by the alcohol dehydrogenase (ADH) and the aldehyde dehydrogenase, both enzymes are membrane-bound and oriented to the periplasmic space. ADH is a quinohemoprotein carrying one pyrroloquinoline quinone moiety, one [2Fe:2S] cluster and four c-type cytochromes, as prosthetic groups. In recent years has been described the presence of the inactive ADH (ADHi) in the acetic acid bacteria. In the present review we make a comparative study of the molecular and catalytic properties of the active and inactive forms of ADH purified from <em>G. diazotrophicus</em>, variation in the redox state of enzymes <em>as purified </em>could explain the notorious differences seen in the activity power of the compared enzymes.

scholarly journals Crystallization of membrane-bound alcohol dehydrogenase of acetic acid bacteria.

1982 ◽  
Vol 46 (11) ◽  
pp. 2859-2863 ◽  
Author(s):  
Osao ADACHI ◽  
Emiko SHINAGAWA ◽  
Kazunobu MATSUSHITA ◽  
Minoru AMEYAMA
Keyword(s):  
Acetic Acid ◽  
Alcohol Dehydrogenase ◽  
Acetic Acid Bacteria ◽  
Membrane Bound

Identifying membrane-bound quinoprotein glucose dehydrogenase from acetic acid bacteria that produce lactobionic and cellobionic acids

2019 ◽  
Vol 83 (6) ◽  
pp. 1171-1179 ◽  
Author(s):  
Takaaki Kiryu ◽  
Taro Kiso ◽  
Daisuke Koma ◽  
Shigemitsu Tanaka ◽  
Hiromi Murakami
Keyword(s):  
Acetic Acid ◽  
Glucose Dehydrogenase ◽  
Acetic Acid Bacteria ◽  
Membrane Bound

scholarly journals Formation of 4-Keto-D-aldopentoses and 4-Pentulosonates (4-Keto-D-pentonates) with Unidentified Membrane-Bound Enzymes from Acetic Acid Bacteria

2011 ◽  
Vol 75 (9) ◽  
pp. 1801-1806 ◽  
Author(s):  
Osao ADACHI ◽  
Roque A. HOURS ◽  
Emiko SHINAGAWA ◽  
Yoshihiko AKAKABE ◽  
Toshiharu YAKUSHI ◽  
...  
Keyword(s):  
Acetic Acid ◽  
Acetic Acid Bacteria ◽  
Membrane Bound ◽  
Membrane Bound Enzymes

scholarly journals A tunable l-arabinose-inducible expression plasmid for the acetic acid bacterium Gluconobacter oxydans

2020 ◽  
Vol 104 (21) ◽  
pp. 9267-9282
Author(s):  
Philipp Moritz Fricke ◽  
Tobias Link ◽  
Jochem Gätgens ◽  
Christiane Sonntag ◽  
Maike Otto ◽  
...  
Keyword(s):  
Acetic Acid ◽  
Stationary Phase ◽  
Gene Knockout ◽  
Glucose Dehydrogenase ◽  
Gluconobacter Oxydans ◽  
Acetic Acid Bacteria ◽  
Acetic Acid Bacterium ◽  
Basal Expression ◽  
Fold Induction ◽  
Membrane Bound

Abstract The acetic acid bacterium (AAB) Gluconobacter oxydans incompletely oxidizes a wide variety of carbohydrates and is therefore used industrially for oxidative biotransformations. For G. oxydans, no system was available that allows regulatable plasmid-based expression. We found that the l-arabinose-inducible PBAD promoter and the transcriptional regulator AraC from Escherichia coli MC4100 performed very well in G. oxydans. The respective pBBR1-based plasmids showed very low basal expression of the reporters β-glucuronidase and mNeonGreen, up to 480-fold induction with 1% l-arabinose, and tunability from 0.1 to 1% l-arabinose. In G. oxydans 621H, l-arabinose was oxidized by the membrane-bound glucose dehydrogenase, which is absent in the multi-deletion strain BP.6. Nevertheless, AraC-PBAD performed similar in both strains in the exponential phase, indicating that a gene knockout is not required for application of AraC-PBAD in wild-type G. oxydans strains. However, the oxidation product arabinonic acid strongly contributed to the acidification of the growth medium in 621H cultures during the stationary phase, which resulted in drastically decreased reporter activities in 621H (pH 3.3) but not in BP.6 cultures (pH 4.4). These activities could be strongly increased quickly solely by incubating stationary cells in d-mannitol-free medium adjusted to pH 6, indicating that the reporters were hardly degraded yet rather became inactive. In a pH-controlled bioreactor, these reporter activities remained high in the stationary phase (pH 6). Finally, we created a multiple cloning vector with araC-PBAD based on pBBR1MCS-5. Together, we demonstrated superior functionality and good tunability of an AraC-PBAD system in G. oxydans that could possibly also be used in other AAB. Key points • We found the AraC-PBADsystem from E. coli MC4100 was well tunable in G. oxydans. •  In the absence of AraC orl-arabinose, expression from PBADwas extremely low. • This araC-PBADsystem could also be fully functional in other acetic acid bacteria.

scholarly journals A New Enzymatic Microdetermination Procedure for Ethanol with Particulate Alcohol Dehydrogenase from Acetic Acid Bacteria

1978 ◽  
Vol 42 (11) ◽  
pp. 2063-2069 ◽  
Author(s):  
Minoru Ameyama ◽  
Kenji Tayama ◽  
Eiji Miyagawa ◽  
Emiko Shinagawa ◽  
Kazunobu Matsushita ◽  
...  
Keyword(s):  
Acetic Acid ◽  
Alcohol Dehydrogenase ◽  
Acetic Acid Bacteria
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