Microbial Production of Methyl Ketones. Purification and Properties of a Secondary Alcohol Dehydrogenase from Yeast

Patel, Ramesh N.; Hou, Ching T.; Laskin, Allen I.; Derelanko, P.; Felix, A.

doi:10.1111/j.1432-1033.1979.tb19732.x

Cited by 44 publications

(27 citation statements)

References 23 publications

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“…In our research, we also found that cell-free extract from H. polymorha P-5 catalyzes the oxidation of a series of alcohols including both primary and secondary alcohols. This is compatible with the previous reports (2,8,9).…”

Section: Discussionsupporting

confidence: 83%

“…The oxidation of primary alcohols other than methanol is catalyzed by a constitutive NAD+-dependent alcohol dehydrogenase (8). Hou et al first discovered and purified a NAD + -specific secondary alcohol dehydrogenase from methanol-grown yeast (2,9). In our research, we also found that cell-free extract from H. polymorha P-5 catalyzes the oxidation of a series of alcohols including both primary and secondary alcohols.…”

Section: Discussionmentioning

confidence: 99%

“…Recently, Hou et al (1,2) discovered that cell suspensions of methanolgrown yeasts catalyze the oxidation of various secondary alcohols to the corresponding methyl ketones. In our studies, we tried to develop this special kind of bioconversion system using immobilized cells.…”

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confidence: 99%

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Oxidation of secondary alcohols to methyl ketones by immobilized yeast cells.

Huang¹,

Fang²,

Fang³

1985

J. Gen. Appl. Microbiol.

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Section: Discussionsupporting

confidence: 83%

Section: Discussionmentioning

confidence: 99%

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Oxidation of secondary alcohols to methyl ketones by immobilized yeast cells.

Huang¹,

Fang²,

Fang³

1985

J. Gen. Appl. Microbiol.

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“…Similar treatment with 750 nmol coppcr yielded spectrum (3). Spectrum (4) shows the absorbance of an eluant fraction. which was observed to bc t'aintly yellow-green Protein C (6 iimol in 1 ml 5 m M , Pipes buffer, pH 7.0) was reduced anaerobically with NADH as previously detailed [14].…”

mentioning

confidence: 99%

“…Copper has been shown to markedly increase the activity of particulate MMO when NADH is supplied as electron donor [2, 31 and this effect has also been observed for particulate extracts of 'Methylosinus' sp. strain CRL-15 [4]. Loss of soluble MMO activity on switching to high copper (1.2 mg Cu2' 1 -I ) medium occurs very rapidly and may be due to inhibition of the enzyme by copper [2].…”

mentioning

confidence: 99%

Copper ions as inhibitors of protein C of soluble methane monooxygenase of Methylococcus capsulatus (Bath)

Green

Prior

Dalton

1985

European Journal of Biochemistry

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Copper(I), copper(I1) and silver ions have been shown to be potent inhibitors of purified soluble methane monooxygenase (MMO) of Methylococcus cupsulatus (Bath). A weaker inhibition has been observed with zinc and cadmium ions. Proteins A and B of soluble MMO are unaffected by copper but protein C is rapidly and irreversibly inhibited. The site of copper inhibition has been shown to be primarily at the iron-sulphur centre of protein C with a secondary effect at the FAD centre when the copper(1I):protein C ratio is high. Copper appears to bring about the inhibition of soluble MMO by interacting with protein C to disrupt the protein structure causing, firstly, the loss of the iron-sulphur centre, preventing the transfer of electrons from protein C to protein A, and secondly, the loss of FAD preventing the protein from accepting electrons from NADH. Inhibition and spectral data are provided to support this thesis. The inactivation of protein C is associated with the tight binding of four Cu atoms to each protein C molecule.These data extend our knowledge of how copper, which is known to have a key role in the cellular location of MMO, interacts with and rapidly and irreversibly inactivates the soluble form of this enzyme.The cellular location of the enzyme methane monooxygenase (MMO) of the obligate methanotroph Methylococcus cupsulatus (Bath), which catalyses the oxidation of methane to methanol, (Eqn 1 [l, 21) has been shown to be dependent on the amount of copper available to the cells during growth.It has recently been demonstrated that at low copper: biomass ratios the predominant form of the enzyme occurs in the soluble fraction of cell extracts and that at high copper: biomass ratios the soluble MMO is inactivated and the particulate, membrane-bound MMO becomes activated [2]. Copper has been shown to markedly increase the activity of particulate MMO when NADH is supplied as electron donor [2, 31 and this effect has also been observed for particulate extracts of 'Methylosinus' sp. strain . Loss of soluble MMO activity on switching to high copper (1.2 mg Cu2' 1 -I ) medium occurs very rapidly and may be due to inhibition of the enzyme by copper [2].The two forms of MMO show marked differences with regard to substrate specificity: the soluble enzyme will oxidize a wide range of alkanes, alkenes, alicyclics and aromatic compounds [5] whereas the particulate enzyme will only oxidize alkanes up to pentane and does not oxidize aromatics under the conditions used in these experiments [7, 81, the predominant form of the enzyme would have been particulate MMO, which is readily inhibited by metal-binding compounds [I]. There have been no reports of inhibition of the soluble MMO by metal ions but it has been demonstrated that soluble MMO is not sensitive to metal chelators [I].Soluble MMO is a multiprotein enzyme consisting of three proteins, all of which are essential for activity [9]. All three proteins have been purified to near homogeneity [lo-141. Protein A is a non-haem-iron protein of M , 210000, which interacts ...

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Secondary Alcohols, Optically Active, Micorbial Production

Yamada‐Onodera

2010

Encyclopedia of Industrial Biotechnology

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The usefulness of optically active substances has been recognized in various fields, and recently the differences between enantiomers are becoming clear especially in medical supplies. The necessity for the enantioselective synthesis has been increasing. The advantages of biocatalysis over chemical synthesis are that enzyme‐catalyzed reactions are highly enantioselective and that they can be performed at ambient temperature and atmospheric pressure, thus avoiding the harsh conditions which cause isomerization, racemization, epimerization, and rearrangement. A lipase has been used to produce optically active secondary alcohols because it has the ability to catalyze hydrolysis of ester bonds with high enantioselectivity. The enantioselective ketone‐reduction and alcohol‐oxidation by secondary alcohol dehydrogenase have been also of interest for the production of various chiral alcohols. Many Alcohol dehydrogenases (ADH) used for this purpose are nicotinamide adenine dinucleotide (NAD) or nicotinamide adenine dinucleotide phosphate (NADP) dependent. Several trials have been achieved for improvement of efficiency mainly in coenzyme recycling. Whole cell reaction is advantageous with respect to saving expensive purification of the desired enzymes. Desired enzymes can be expressed in transformants to make biocatalytic processes economically efficient. Preparative application for industrial purpose will be demonstrated.

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Microbial Production of Methyl Ketones. Purification and Properties of a Secondary Alcohol Dehydrogenase from Yeast

Cited by 44 publications

References 23 publications

Oxidation of secondary alcohols to methyl ketones by immobilized yeast cells.

Oxidation of secondary alcohols to methyl ketones by immobilized yeast cells.

Copper ions as inhibitors of protein C of soluble methane monooxygenase of Methylococcus capsulatus (Bath)

Secondary Alcohols, Optically Active, Micorbial Production

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