Methanol dehydrogenase: Mechanism of action
In: Antonie van Leeuwenhoek, Jg. 56 (1989-05-01), S. 25-34
Online
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Zugriff:
Methanol dehydrogenase (MDH, EC 1.1.99.8) was first described in 1964 by Anthony and Zatman (Anthony and Zatman 1964, 1965, 1967a,b). Since that time a large number of MDH’s have been found with similar properties (Anthony 1986) including the dimeric MDH from Hyphomicrobium X (Duine et al. 1978). Methanol dehydrogenases are dye-linked enzymes, efficient electron transfer occurring exclusively to cationic electron acceptors at relatively high pH values (> 9). Enzymatic activity requires the presence of ammonia and sometimes higher amines as activators. Like many other quinoproteins, MDH’s are characterized by a broad substrate specificity, besides methanol a wide range of primary alcohols is oxidized and some enzymes also oxidize secondary alcohols. Formaldehyde, and sometimes acetaldehyde, is also a substrate. Modulation of the substrate specificity by a modifier protein has been observed in several organisms (Bolbot and Anthony, 1980) and it has been suggested that this protein functions as a regulator of formaldehyde oxidation.
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Methanol dehydrogenase: Mechanism of action
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Autor/in / Beteiligte Person: | Duine, Johannis A. ; Frank, Jeroen ; Balny, Claude ; Verwiel, P. E. J. ; Dijkstra, M. |
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Zeitschrift: | Antonie van Leeuwenhoek, Jg. 56 (1989-05-01), S. 25-34 |
Veröffentlichung: | Springer Science and Business Media LLC, 1989 |
Medientyp: | unknown |
ISSN: | 1572-9699 (print) ; 0003-6072 (print) |
DOI: | 10.1007/bf00822581 |
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