Liver alcohol dehydrogenase from Equus caballus (horse)

Enzyme Description

Extremophile
No
EC Number

Sequence

Length: 375 amino acids
MSTAGKVIKCKAAVLWEEKKPFSIEEVEVAPPKAHEVRIKMVATGICRSDDHVVSGTLVTPLPVIAGHEAAGIVESIGEGVTTVRPGDKVIPLFTPQCGKCRVCKHPEGNFCLKNDLSMPRGTMQDGTSRFTCRGKPIHHFLGTSTFSQYTVVDEISVAKIDAASPLEKVCLIGCGFSTGYGSAVKVAKVTQGSTCAVFGLGGVGLSVIMGCKAAGAARIIGVDINKDKFAKAKEVGATECVNPQDYKKPIQEVLTEMSNGGVDFSFEVIGRLDTMVTALSCCQEAYGVSVIVGVPPDSQNLSMNPMLLLSGRTWKGAIFGGFKSKDSVPKLVADFMAKKFALDPLITHVLPFEKINEGFDLLRSGESIRTILTF
Annika Johansson et al. (1995) β€” Horse Liver Alcohol Dehydrogenase can Accept NADP+ as Coenzyme in High Concentrations of Acetonitrile
European Journal of Biochemistry  Β· doi:10.1111/j.1432-1033.1995.tb20423.x β†—  Β· Activity - Classical
8 measurements
Database ID
UniProt: P00327 β†—
Sequence Annotation
Inferred - from protein name
Protein Source
Commercially purchased

Experimental Data (8 measurements)

8 measurements
Property Assay Solvent Solvent Volume Aqueous Reference Measured Value Units Solution pH Temperature Substrate(s) Product(s) Cofactor(s) Shaking Comments
Activity - Classical Activity (in units of nmol*min^-1*mg*enzyme^-1) measured by HPLC in the presence of organic solvent Acetonitrile 98% 1200.0 1.0 nmol/(min*mg) 10 mM Tris-HCl buffer, 10 mM octanal (cofactor recycling) 7.4 Room temperature 10 mM Cinnamoyl alcohol Cinnamaldehyde NAD+ β€” Classical aqueous control (in nmol/(min*mg))
Activity - Classical Activity (in units of nmol*min^-1*mg*enzyme^-1) measured by HPLC in the presence of organic solvent Acetonitrile 95% 1200.0 1.6 nmol/(min*mg) 10 mM Tris-HCl buffer, 10 mM octanal (cofactor recycling) 7.4 Room temperature 10 mM Cinnamoyl alcohol Cinnamaldehyde NAD+ β€” Classical aqueous control (in nmol/(min*mg))
Activity - Classical Activity (in units of nmol*min^-1*mg*enzyme^-1) measured by HPLC in the presence of organic solvent Acetonitrile 90% 1200.0 8.6 nmol/(min*mg) 10 mM Tris-HCl buffer, 10 mM octanal (cofactor recycling) 7.4 Room temperature 10 mM Cinnamoyl alcohol Cinnamaldehyde NAD+ β€” Classical aqueous control (in nmol/(min*mg))
Activity - Classical Activity (in units of nmol*min^-1*mg*enzyme^-1) measured by HPLC in the presence of organic solvent Acetonitrile 75% 1200.0 18.3 nmol/(min*mg) 10 mM Tris-HCl buffer, 10 mM octanal (cofactor recycling) 7.4 Room temperature 10 mM Cinnamoyl alcohol Cinnamaldehyde NAD+ β€” Classical aqueous control (in nmol/(min*mg))
Activity - Classical Activity (in units of nmol*min^-1*mg*enzyme^-1) measured by HPLC in the presence of organic solvent Acetonitrile 98% 45.0 2.4 nmol/(min*mg) 10 mM Tris-HCl buffer, 10 mM octanal (cofactor recycling) 7.4 Room temperature 10 mM Cinnamoyl alcohol Cinnamaldehyde NADP+ β€” Classical aqueous control (in nmol/(min*mg))
Activity - Classical Activity (in units of nmol*min^-1*mg*enzyme^-1) measured by HPLC in the presence of organic solvent Acetonitrile 95% 45.0 6.8 nmol/(min*mg) 10 mM Tris-HCl buffer, 10 mM octanal (cofactor recycling) 7.4 Room temperature 10 mM Cinnamoyl alcohol Cinnamaldehyde NADP+ β€” Classical aqueous control (in nmol/(min*mg))
Activity - Classical Activity (in units of nmol*min^-1*mg*enzyme^-1) measured by HPLC in the presence of organic solvent Acetonitrile 90% 45.0 11.8 nmol/(min*mg) 10 mM Tris-HCl buffer, 10 mM octanal (cofactor recycling) 7.4 Room temperature 10 mM Cinnamoyl alcohol Cinnamaldehyde NADP+ β€” Classical aqueous control (in nmol/(min*mg))
Activity - Classical Activity (in units of nmol*min^-1*mg*enzyme^-1) measured by HPLC in the presence of organic solvent Acetonitrile 75% 45.0 1.1 nmol/(min*mg) 10 mM Tris-HCl buffer, 10 mM octanal (cofactor recycling) 7.4 Room temperature 10 mM Cinnamoyl alcohol Cinnamaldehyde NADP+ β€” Classical aqueous control (in nmol/(min*mg))

Visualization : Activity β€” Classical

Annika Johansson et al. (1995)

One bar per measurement. Colour = solvent, shade = solvent volume.

Daria Giacomini et al. (2007) β€” Highly efficient asymmetric reduction of arylpropionic aldehydes by Horse Liver Alcohol Dehydrogenase through dynamic kinetic resolution
Chemical Communications  Β· doi:10.1039/b712290j β†—  Β· Activity + Stability - Product Formation
7 measurements
Leanne M. Timpson et al. (2011) β€” Characterization of alcohol dehydrogenase (ADH12) from Haloarcula marismortui, an extreme halophile from the Dead Sea
Extremophiles  Β· doi:10.1007/s00792-011-0405-0 β†—  Β· Stability - Incubation
2 measurements
Leanne M. Timpson et al. (2012) β€” A comparison of two novel alcohol dehydrogenase enzymes (ADH1 and ADH2) from the extreme halophile Haloferax volcanii
Applied Microbiology and Biotechnology  Β· doi:10.1007/s00253-012-4074-4 β†—  Β· Stability - Incubation
5 measurements
Ningning Zhang et al. (2022) β€” Unraveling Alcohol Dehydrogenase Catalysis in Organic–Aqueous Biphasic Systems Combining Experiments and Molecular Dynamics Simulations
ACS Catalysis  Β· doi:10.1021/acscatal.2c02881 β†—  Β· Activity - Classical Activity + Stability - Product Formation Specificity - Enantioselectivity Stability - Half-life
35 measurements

Structure

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