scholarly journals Investigating inducible short-chain alcohol dehydrogenases/reductases clarifies rice oryzalexin biosynthesis

2016 ◽  
Vol 88 (2) ◽  
pp. 271-279 ◽  
Author(s):  
Naoki Kitaoka ◽  
Yisheng Wu ◽  
Jiachen Zi ◽  
Reuben J. Peters
Keyword(s):  
Short Chain ◽  
Alcohol Dehydrogenases ◽  
Chain Alcohol ◽  
Short Chain Alcohol

scholarly journals Characteristics of short-chain alcohol dehydrogenases and related enzymes

1991 ◽  
Vol 200 (2) ◽  
pp. 543-543
Author(s):  
Bengt PERSSON ◽  
Maria KROOK ◽  
Hans JORNVALL
Keyword(s):  
Short Chain ◽  
Alcohol Dehydrogenases ◽  
Chain Alcohol ◽  
Short Chain Alcohol

Characteristics of short-chain alcohol dehydrogenases and related enzymes

1991 ◽  
Vol 200 (2) ◽  
pp. 537-543 ◽  
Author(s):  
Bengt PERSSON ◽  
Maria KROOK ◽  
Hans JORNVALL
Keyword(s):  
Short Chain ◽  
Alcohol Dehydrogenases ◽  
Chain Alcohol ◽  
Short Chain Alcohol

scholarly journals The Retinal Pigment Epithelial-specific 11-cisRetinol Dehydrogenase Belongs to the Family of Short Chain Alcohol Dehydrogenases

1995 ◽  
Vol 270 (3) ◽  
pp. 1107-1112 ◽  
Author(s):  
Andràs Simon ◽  
Ulf Hellman ◽  
Christer Wernstedt ◽  
Ulf Eriksson
Keyword(s):  
Retinal Pigment Epithelial ◽  
Retinal Pigment ◽  
Short Chain ◽  
Alcohol Dehydrogenases ◽  
Chain Alcohol ◽  
Pigment Epithelial ◽  
The Family ◽  
Short Chain Alcohol

scholarly journals Structural properties of long- and short-chain alcohol dehydrogenases. Contribution of NAD+ to stability

1991 ◽  
Vol 276 (2) ◽  
pp. 433-438 ◽  
Author(s):  
L Ribas De Pouplana ◽  
S Atrian ◽  
R Gonzàlex-Duarte ◽  
L A Fothergill-Gilmore ◽  
S M Kelly ◽  
...  
Keyword(s):  
Liver Enzyme ◽  
Structure Prediction ◽  
State Model ◽  
Short Chain ◽  
Alcohol Dehydrogenases ◽  
Chain Alcohol ◽  
Horse Liver ◽  
Short Chain Alcohol ◽  
Two State Model ◽  
Good Agreement

Structural studies were undertaken on long-chain and short-chain alcohol dehydrogenases (from horse liver and Drosophila respectively). Far-u.v. c.d. measurements were used to estimate the secondary structure contents of the enzymes. For the horse liver enzyme, the results agree well with the X-ray data; for the Drosophila enzyme (for which a crystal structure is not yet available), the results are in good agreement with those obtained by applying a range of structure-prediction procedures to the amino acid sequence of this enzyme. The conformational stabilities of the two enzymes were investigated by studying the unfolding brought about by guanidinium chloride (GdnHCl) by using activity and c.d. measurements. The unfolding of the Drosophila enzyme was analysed in terms of a two-state model; the presence of the substrate NAD+ leads to considerable protection against unfolding. By contrast, the unfolding of the horse liver enzyme shows a plateau effect at intermediate concentrations of GdnHCl, indicating that a two-state model is not appropriate in this case. NAD+ affords little, if any, protection against unfolding for the horse liver enzyme.

scholarly journals The Extra Loop Distinguishing POR from the Structurally Related Short-chain Alcohol Dehydrogenases Is Dispensable for Pigment Binding but Needed for the Assembly of Light-harvesting POR-Protochlorophyllide Complex

2002 ◽  
Vol 278 (2) ◽  
pp. 816-822 ◽  
Author(s):  
Christiane Reinbothe ◽  
Anja Lepinat ◽  
Markus Deckers ◽  
Erwin Beck ◽  
Steffen Reinbothe
Keyword(s):  
Light Harvesting ◽  
Short Chain ◽  
Alcohol Dehydrogenases ◽  
Chain Alcohol ◽  
Short Chain Alcohol

scholarly journals Theoretical Calculations of the Catalytic Triad in Short-Chain Alcohol Dehydrogenases/Reductases

2008 ◽  
Vol 94 (4) ◽  
pp. 1412-1427 ◽  
Author(s):  
Osman A.B.S.M. Gani ◽  
Olayiwola A. Adekoya ◽  
Laura Giurato ◽  
Francesca Spyrakis ◽  
Pietro Cozzini ◽  
...  
Keyword(s):  
Theoretical Calculations ◽  
Catalytic Triad ◽  
Short Chain ◽  
Alcohol Dehydrogenases ◽  
Chain Alcohol ◽  
Short Chain Alcohol
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