An effective hybrid strategy for converting rice straw to furoic acid by tandem catalysis via Sn-sepiolite combined with recombinant E. coli whole cells harboring horse liver alcohol dehydrogenase

2019 ◽  
Vol 21 (21) ◽  
pp. 5914-5923 ◽  
Author(s):  
Bo Peng ◽  
Cui-Luan Ma ◽  
Peng-Qi Zhang ◽  
Chang-Qing Wu ◽  
Zi-Wei Wang ◽  
...  
Keyword(s):  
Alcohol Dehydrogenase ◽  
Rice Straw ◽  
Tandem Catalysis ◽  
Horse Liver Alcohol Dehydrogenase ◽  
Hybrid Strategy ◽  
Furoic Acid ◽  
Whole Cells ◽  
E Coli ◽  
Liver Alcohol Dehydrogenase ◽  
Horse Liver

The upgrading of biomass-derived furfural into high-value bio-based chemicals has attracted interest.

scholarly journals Binding of substrate in a ternary complex of horse liver alcohol dehydrogenase.

1982 ◽  
Vol 257 (23) ◽  
pp. 14349-14358 ◽  
Author(s):  
H Eklund ◽  
B V Plapp ◽  
J P Samama ◽  
C I Brändén
Keyword(s):  
Alcohol Dehydrogenase ◽  
Ternary Complex ◽  
Horse Liver Alcohol Dehydrogenase ◽  
Liver Alcohol Dehydrogenase ◽  
Horse Liver

Coordination geometry for cadmium in the catalytic zinc site of horse liver alcohol dehydrogenase: studies by PAC spectroscopy

1991 ◽  
Vol 20 (4) ◽  
Author(s):  
R. Bauer ◽  
H.W. Adolph ◽  
I. Andersson ◽  
E. Danielsen ◽  
G. Formicka ◽  
...  
Keyword(s):  
Alcohol Dehydrogenase ◽  
Coordination Geometry ◽  
Pac Spectroscopy ◽  
Horse Liver Alcohol Dehydrogenase ◽  
Liver Alcohol Dehydrogenase ◽  
Horse Liver ◽  
Catalytic Zinc ◽  
Zinc Site

scholarly journals Horse liver alcohol dehydrogenase. A study of the essential lysine residue

1975 ◽  
Vol 149 (3) ◽  
pp. 627-635 ◽  
Author(s):  
S S Chen ◽  
P C Engel
Keyword(s):  
Alcohol Dehydrogenase ◽  
Rate Constant ◽  
Lysine Residue ◽  
Horse Liver Alcohol Dehydrogenase ◽  
First Order ◽  
Liver Alcohol Dehydrogenase ◽  
Horse Liver ◽  
Lysine Residues ◽  
Modified Enzyme ◽  
Covalent Complex

1. The inactivation of horse liver alcohol dehydrogenase by pyridoxal 5'-phosphate in phosphate buffer, pH8, at 10°C was investigated. Activity declines to a minimum value determined by the pyridoxal 5'-phosphate concentration. The maximum inactivation in a single treatment is 75%. This limit appears to be set by the ratio of the first-order rate constants for interconversion of inactive covalently modified enzyme and a readily dissociable non-covalent enzyme-modifier complex. 2. Reactivation was virtually complete on 150-fold dilution: first-order analysis yielded an estimate of the rate constant (0.164min-1), which was then used in the kinetic analysis of the forward inactivation reaction. This provided estimates for the rate constant for conversion of non-covalent complex into inactive enzyme (0.465 min-1) and the dissociation constant of the non-covalent complex (2.8 mM). From the two first-order constants, the minimum attainable activity in a single cycle of treatment may be calculated as 24.5%, very close to the observed value. 3. Successive cycles of modification followed by reduction with NaBH4 each decreased activity by the same fraction, so that three cycles with 3.6 mM-pyridoxal 5'-phosphate decreased specific activity to about 1% of the original value. The absorption spectrum of the enzyme thus treated indicated incorporation of 2-3 mol of pyridoxal 5'-phosphate per mol of subunit, covalently bonded to lysine residues. 4. NAD+ and NADH protected the enzyme completely against inactivation by pyridoxal 5'-phosphate, but ethanol and acetaldehyde were without effect. 5. Pyridoxal 5'-phosphate used as an inhibitor in steady-state experiments, rather than as an inactivator, was non-competitive with respect to both NADH and acetaldehyde. 6. The partially modified enzyme (74% inactive) showed unaltered apparent Km values for NAD+ and ethanol, indicating that modified enzyme is completely inactive, and that the residual activity is due to enzyme that has not been covalently modified. 7. Activation by methylation with formaldehyde was confirmed, but this treatment does not prevent subsequent inactivation with pyridoxal 5'-phosphate. Presumably different lysine residues are involved. 8. It is likely that the essential lysine residue modified by pyridoxal 5'-phosphate is involved either in binding the coenzymes or in the catalytic step. 9. Less detailed studies of yeast alcohol dehydrogenase suggest that this enzyme also possesses an essential lysine residue.

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