A novel, efficient regenerating method of NADPH using a new formate dehydrogenase

doi:10.1016/0040-4039(96)00010-X

Tetrahedron Letters

Volume 37, Issue 9, 26 February 1996, Pages 1377-1380

https://doi.org/10.1016/0040-4039(96)00010-X Get rights and content

Abstract

A NADPH regenerating system using a new, protein engineered formate dehydrogenase (FDH) is investigated. The new enzyme is the first known NAD(P)H dependent FDH. It can be successfully employed in synthesis with other enzymes requiring a NADPH regeneration. All advantages of the known NAD(H) dependent FDH's in these enzyme coupled synthesis can now be transferred to NADP(H) dependent systems.

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References (29)

A. Fry et al.
Tetrahedron Lett.
(1994)
M.-R. Kula et al.
Methods Enzymol.
(1987)
M.-R. Kula
Enzyme Catalyzed Reductions of Carbonyl Groups
Kragl, U.; Kruse, W.; Hummel, W; Wandrey, C. Biotech. Bioeng., accepted for...
H.K. Chenault et al.
Appl. Microbiol. Biotech.
(1987)
R. Ruppert et al.
J. Chem. Soc. Chem. Commun.
(1988)
Y. Morita et al.
J. Ferment. Bioeng.
(1994)
K. Nakamura et al.
Electroenzymology Coenzyme Regeneration
(1988)
C.-H. Wong et al.
Enzymes in Organic Chemistry
(1994)
C.-H. Wong et al.
J. Am. Chem. Soc.
(1981)

C.-H. Wong et al.

J. Org. Chem.

(1982)

W. Hummel

Appl. Microbiol. Biotech.

(1990)

W. Hummel

J. Biotech. Lett.

(1990)

E. Keinan et al.

J. Am. Chem. Soc.

(1986)

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A novel, efficient regenerating method of NADPH using a new formate dehydrogenase

Abstract

Tetrahedron Lett.

Methods Enzymol.

Enzyme Catalyzed Reductions of Carbonyl Groups

Appl. Microbiol. Biotech.

J. Chem. Soc. Chem. Commun.

J. Ferment. Bioeng.

Electroenzymology Coenzyme Regeneration

Enzymes in Organic Chemistry

J. Am. Chem. Soc.

J. Org. Chem.

Appl. Microbiol. Biotech.

J. Biotech. Lett.

J. Am. Chem. Soc.