1.1.1.2: alcohol dehydrogenase (NADP+)

This is an abbreviated version, for detailed information about alcohol dehydrogenase (NADP+), go to the full flat file.

Reaction

a primary alcohol
+
NADP+
=
an aldehyde
+
NADPH
+
H+

Synonyms

2 Adh, 3-DG-reducing enzyme, AAur_2040, ADH, ADH-1, ADH-2, ADH-I, ADH-II, ADH2, Adh319, ADH4, Adh6, AdhA, AdhB, AKR1A1, AKR1A4, alcohol dehydrogenase C, alcohol dehydrogenase [NADP(+)], Alcohol dehydrogenase [NADP+], aldehyde reductase, aldehyde reductase (NADPH2), aldehyde/ketone reductase, aldo-keto reductase, Aldo-keto reductase family 1 member A1, aldose reductase, ALDR, alipathic aldehyde reductase, ALR, ALR 1, ALR1, BdhA, bovine brain aldehyde reductase, D-glucuronate reductase, daunorubicin reductase, DRD, EhADH1, Gre2p, hexogenate dehydrogenase, high-Km aldehyde reductase, HvADH2, L-hexonate dehydrogenase, LB-RADH, LBADH, liver alcohol dehydrogenase, low-Km aldehyde reductase, mevaldate reductase, Mpd1, NADP(H)-dependent alcohol dehydrogenase, NADP-alcohol dehydrogenase, NADP-aldehyde reductase, NADP-dependent aldehyde reductase, NADP-linked aryl alcohol dehydrogenase, NADPH-aldehyde reductase, NADPH-cytochrome c reductase, NADPH-dependent aldehyde reductase, NADPH-dependent FALDR, NADPH-dependent fatty aldehyde reductase, NADPH-linked aldehyde reductase, nonspecific succinic semialdehyde reductase, Octopine dehydrogenase, putative iron alcohol dehydrogenase, PyAeADHII, rabbit kidney aldehyde-ketone reductase, RADH, ScADHVI, short-chain ADH, short-chain alcohol dehydrogenase, short-chain dehydrogenase/reductase, TBADH, TbADH1, Teth39_1597, Teth514_0564, TPN-L-hexonate dehydrogenase, TPNH-linked aldehyde reductase, TPNH-specific aldehyde reductase, triphosphopyridine nucleotide-linked aldehyde reductase, TsAdh319, Y63 protein, yeast alcohol dehydrogenase, YqhD

ECTree

     1 Oxidoreductases
         1.1 Acting on the CH-OH group of donors
             1.1.1 With NAD+ or NADP+ as acceptor
                1.1.1.2 alcohol dehydrogenase (NADP+)

Engineering

Engineering on EC 1.1.1.2 - alcohol dehydrogenase (NADP+)

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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
D275P
mutation significantly enhances the thermal stability of EhADH1
G37D
-
regular PCR with site-specific mutation for both DNA strands, the gene is divided into two separate amplification products, preference for NAD+ rather than NADP+, depends on an a interaction between the adenosine ribose moiety of NAD+ and the inserted aspartate side chain
D194A
mutation in putative metal-coordinating residue, almost complete loss of activity
H198A
mutation in putative metal-coordinating residue, almost complete loss of activity
H267A
mutation in putative metal-coordinating residue, almost complete loss of activity
H281A
mutation in putative metal-coordinating residue, almost complete loss of activity
H363A
107% of wild-type activity
D194A
-
mutation in putative metal-coordinating residue, almost complete loss of activity
-
H198A
-
mutation in putative metal-coordinating residue, almost complete loss of activity
-
H267A
-
mutation in putative metal-coordinating residue, almost complete loss of activity
-
H281A
-
mutation in putative metal-coordinating residue, almost complete loss of activity
-
H363A
-
107% of wild-type activity
-
K245R
-
mutation leads to improved thermostability
L54Q
-
mutant retains 62% of its initial activity after heat treatment at 30C for 6 h and mutation confers improved enantioselectivity
L54Q/K245R/N271D
-
mutant displays improved thermostability and mutation confers improved enantioselectivity
L54Q/R104C
-
mutation leads to improved thermostability and enantioselectivity
N271D
-
mutation leads to improved thermostability
K245R
-
mutation leads to improved thermostability
-
L54Q
-
mutant retains 62% of its initial activity after heat treatment at 30C for 6 h and mutation confers improved enantioselectivity
-
L54Q/K245R/N271D
-
mutant displays improved thermostability and mutation confers improved enantioselectivity
-
L54Q/R104C
-
mutation leads to improved thermostability and enantioselectivity
-
N271D
-
mutation leads to improved thermostability
-
A18P/K40N/Q165H/D182H/E202G/R219M
-
mutant with increased specific activity towards 2,5-hexanedione compared to the wild type enzyme
K209T
-
mutant with wild type specific activity towards 2,5-hexanedione
L176P
-
mutant with the highest activity at 30C with 2,5-hexanedione, the temperature optimum of the mutant is not changed (90C), but the activity at lower temperature (60C and below) is clearly increased when compared to the wild type enzyme
N86D/R213I
-
mutant with increased specific activity towards 2,5-hexanedione compared to the wild type enzyme
R11L/A180V
-
mutant with the highest activity at 30C with 2,5-hexanedione, the temperature optimum of the mutant is not changed (90C), but the activity at lower temperature (60C and below) is clearly increased when compared to the wild type enzyme, the maximum specific activity of R11L/A180V with 2,5-hexanedione at 30C is 10fold higher compared to the activity of the wild type enzyme; the maximum specific activity of the mutant with 2,5-hexanedione at 30C is 10fold higher compared to the activity of the wild type enzyme
T153A
-
mutant with the highest activity at 30C with 2,5-hexanedione, the temperature optimum of the mutant is not changed (90C), but the activity at lower temperature (60C and below) is clearly increased when compared to the wild type enzyme
V66A/L176P/Y229H
-
mutant with increased specific activity towards 2,5-hexanedione compared to the wild type enzyme
P275D
mutation reduces the thermostability of the enzyme
W110A
-
99.9% conversion of phenylacetone to 84.1% S-product
W110G
-
99.9% conversion of phenylacetone to 79% S-product, 95.8% conversion of 1-phenyl-2-butanone to 91.6% S-product, 99.1% conversion of 4-phenyl-2-butanone to 70.5% S-product
W110I
-
99.9% conversion of phenylacetone to 99.9% S-product, 99.4% conversion of 1-phenyl-2-butanone to 99.9% S-product, 99.1% conversion of 4-phenyl-2-butanone to 99.9% S-product
W110L
-
99.9% conversion of phenylacetone to 99.9% S-product, 98.9% conversion of 1-phenyl-2-butanone to 99.9% S-product, 99.2% conversion of 4-phenyl-2-butanone to 99.9% S-product
W110M
-
99.9% conversion of phenylacetone to 99.9% S-product, 97.3% conversion of 1-phenyl-2-butanone to 99.9% S-product, 99.3% conversion of 4-phenyl-2-butanone to 99.9% S-product
W110Q
-
99.9% conversion of phenylacetone to 99.9% S-product, 83.5% conversion of 1-phenyl-2-butanone to 99.9% S-product, 99.1% conversion of 4-phenyl-2-butanone to 99.9% S-product
W110V
-
99.9% conversion of phenylacetone to 99.9% S-product, 99.2% conversion of 1-phenyl-2-butanone to 99.9% S-product, 99.1% conversion of 4-phenyl-2-butanone to 99.9% S-product
additional information