Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 1.1.1.71 extracted from

  • Bartsch, S.; Brummund, J.; Koepke, S.; Straatman, H.; Vogel, A.; Schuermann, M.
    Optimization of alcohol dehydrogenase for industrial scale oxidation of lactols (2020), Biotechnol. J., 15, e2000171 .
    View publication on PubMed
Search for more literature for 1.1.1.71

Protein Variants

Protein Variants Comment Organism
E43K/S97C/T148S/A155H/P210C/L227V/Y244F site-directed mutagenesis, mutant ADHA-0381, the mutant shows increased thermostability and altered pH conditions compared to the wild-type enzyme Starmerella magnoliae
E43K/S97C/T148S/T194V/M206D/P210C/L227V site-directed mutagenesis, mutant ADHA-0398, the mutant shows increased thermostability and altered pH conditions compared to the wild-type enzyme Starmerella magnoliae
additional information development of improved enzyme variants ADHA-0398 and -0381 shows +26°C improved melting temperature and 17fold higher oxidative activity at pH 6.5 towards (4R,6S)-6-(chloromethyl)oxane-2,4-diol but only 6fold at pH 7.5, method development, overview Starmerella magnoliae
S97C/M206D site-directed mutagenesis, mutant ADHA-0279, the mutant shows increased thermostability and altered pH conditions compared to the wild-type enzyme Starmerella magnoliae
S97C/M206D/P210C site-directed mutagenesis, mutant ADHA-0278, the mutant shows increased thermostability and altered pH conditions compared to the wild-type enzyme Starmerella magnoliae
S97C/T148S/A155H/P210C/L227V site-directed mutagenesis, mutant ADHA-0391, the mutant shows increased thermostability and altered pH conditions compared to the wild-type enzyme Starmerella magnoliae
S97C/T148S/A155H/P210C/L227V/Y244F site-directed mutagenesis, mutant ADHA-0384, the mutant shows increased thermostability and altered pH conditions compared to the wild-type enzyme Starmerella magnoliae

Organism

Organism UniProt Comment Textmining
Starmerella magnoliae
-
-
-
Starmerella magnoliae DSMZ 70638
-
-
-

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
additional information
-
 specific activities of enzyme mutants with the different substrates, overview Starmerella magnoliae
0.33
-
 wild-type enzyme, pH 6.5, 28°C, substrate (4R,6S)-6-(chloromethyl)oxane-2,4-diol Starmerella magnoliae
4.11
-
 wild-type enzyme, pH 7.0, 28°C, substrate ethyl acetoacetate Starmerella magnoliae
4.11
-
 wild-type enzyme, pH 7.5, 28°C, substrate (4R,6S)-6-(chloromethyl)oxane-2,4-diol Starmerella magnoliae
12.9
-
 wild-type enzyme, pH 7.0, 28°C, substrate (4R,6R)-6-butyloxane-2,4-diol Starmerella magnoliae

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
(4R,6R)-6-butyloxane-2,4-diol + NAD+
-
 Starmerella magnoliae (4R,6R)-6-butyl-4-hydroxyoxan-2-one + NADH + H+
-
 ?
(4R,6R)-6-butyloxane-2,4-diol + NAD+
-
 Starmerella magnoliae DSMZ 70638 (4R,6R)-6-butyl-4-hydroxyoxan-2-one + NADH + H+
-
 ?
(4R,6R)-6-butyloxane-2,4-diol + NADP+
-
 Starmerella magnoliae (4R,6R)-6-butyl-4-hydroxyoxan-2-one + NADPH + H+
-
 ?
(4R,6R)-6-butyloxane-2,4-diol + NADP+
-
 Starmerella magnoliae DSMZ 70638 (4R,6R)-6-butyl-4-hydroxyoxan-2-one + NADPH + H+
-
 ?
(4R,6R)-6-pentyloxane-2,4-diol + NAD+
-
 Starmerella magnoliae (4R,6R)-4-hydroxy-6-pentyloxan-2-one + NADH + H+
-
 ?
(4R,6R)-6-pentyloxane-2,4-diol + NAD+
-
 Starmerella magnoliae DSMZ 70638 (4R,6R)-4-hydroxy-6-pentyloxan-2-one + NADH + H+
-
 ?
(4R,6R)-6-pentyloxane-2,4-diol + NADP+
-
 Starmerella magnoliae (4R,6R)-4-hydroxy-6-pentyloxan-2-one + NADPH + H+
-
 ?
(4R,6R)-6-pentyloxane-2,4-diol + NADP+
-
 Starmerella magnoliae DSMZ 70638 (4R,6R)-4-hydroxy-6-pentyloxan-2-one + NADPH + H+
-
 ?
(4R,6S)-6-(chloromethyl)oxane-2,4-diol + NAD+
-
 Starmerella magnoliae (4R,6S)-6-(chloromethyl)-4-hydroxyoxan-2-one + NADH + H+
-
 ?
(4R,6S)-6-(chloromethyl)oxane-2,4-diol + NADP+
-
 Starmerella magnoliae (4R,6S)-6-(chloromethyl)-4-hydroxyoxan-2-one + NADPH + H+
-
 ?
ethyl acetoacetate + NADPH + H+
-
 Starmerella magnoliae ? + NADP+
-
 r
additional information lactol substrates (4R,6S)-6-(chloromethyl)oxane-2,4-diol and (4R,6R)-6-butyloxane-2,4-diol for the biocatalytic oxidations are obtained from 2-deoxy-D-ribose 5-phosphate aldolase (DERA) catalyzed reactions of the corresponding acceptor aldehydes chloroacetaldehyde and pentanal, respectively and at least two equivalents of acetaldehyde as described previously. Development of an efficient biocatalytic process on pilot plant scale to oxidize the aliphatic hydroxylactol substrate (4R,6R)-6-butyloxane-2,4-diol to the corresponding lactone product (4R,6R)-6-butyl-4-hydroxyoxan-2-one employing the wild-type alcohol dehydrogenase ADHA Starmerella magnoliae ?
-
-
additional information lactol substrates (4R,6S)-6-(chloromethyl)oxane-2,4-diol and (4R,6R)-6-butyloxane-2,4-diol for the biocatalytic oxidations are obtained from 2-deoxy-D-ribose 5-phosphate aldolase (DERA) catalyzed reactions of the corresponding acceptor aldehydes chloroacetaldehyde and pentanal, respectively and at least two equivalents of acetaldehyde as described previously. Development of an efficient biocatalytic process on pilot plant scale to oxidize the aliphatic hydroxylactol substrate (4R,6R)-6-butyloxane-2,4-diol to the corresponding lactone product (4R,6R)-6-butyl-4-hydroxyoxan-2-one employing the wild-type alcohol dehydrogenase ADHA Starmerella magnoliae DSMZ 70638 ?
-
-

Synonyms

Synonyms Comment Organism
ADH
-
 Starmerella magnoliae
AdhA
-
 Starmerella magnoliae
alcohol dehydrogenase
-
 Starmerella magnoliae
NADPH-dependent ADHA
-
 Starmerella magnoliae

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
28 42 assay at Starmerella magnoliae

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
41
-
 melting temperature T1/2 of wild-type enzyme ADHA Starmerella magnoliae
48
-
 melting temperature T1/2 of mutant ADHA-0278 Starmerella magnoliae
53
-
 melting temperature T1/2 of mutant ADHA-0279 Starmerella magnoliae
65
-
 melting temperature T1/2 of mutant ADHA-0391 Starmerella magnoliae
66
-
 melting temperature T1/2 of mutant ADHA-0384 Starmerella magnoliae
67
-
 melting temperature T1/2 of mutant ADHA-0398 and of mutant ADHA-0381 Starmerella magnoliae

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
6.5 7.5 dependent on the substrate Starmerella magnoliae

Cofactor

Cofactor Comment Organism Structure
NAD+
-
 Starmerella magnoliae
NADH
-
 Starmerella magnoliae
NADP+
-
 Starmerella magnoliae
NADPH
-
 Starmerella magnoliae

General Information

General Information Comment Organism
malfunction the optimized ADHA variant shows a 7fold higher oxidative activity, a 26°C increased stability, and is applied to develop an efficient chlorolactol oxidation process Starmerella magnoliae
physiological function enzyme ADHA from Candida magnoliae strain DSMZ 70638 is identified to efficiently catalyze the regioselective hydroxy-lactone oxidations to hydroxy-lactones. Hydroxy-lactones are common intermediates in industrial processes to cholesterol lowering (va)statin drugs. ADH catalyzed oxidations can be developed to efficient and safe processes, but the ADHA wild-type enzyme is not productive enough in chlorolactol oxidation Starmerella magnoliae