A comparison of the substrate and electron-donor specificities of the methane mono-oxygenases from three strains of methane-oxidizing bacteria

1. Methane mono-oxygenase from Methylosinus trichosporium has the same broad substrate specificity as the analogous enzyme from Methylococcus capsulatus (Bath); the enzyme from Methylomonas methanica is more specific. 2. Contrary to previous reports, NAD(P)H and not ascorbate is the required electron donor for the enzyme from Methylosinus trichosporium. 3. It is concluded that these three bacteria contain similar methane mono-oxygenases.

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The soluble methane mono-oxygenase of Methylococcus capsulatus (Bath). Its ability to oxygenate n-alkanes, n-alkenes, ethers, and alicyclic, aromatic and heterocyclic compounds

Biochemical Journal ◽

10.1042/bj1650395 ◽

1977 ◽

Vol 165 (2) ◽

pp. 395-402 ◽

Cited By ~ 364

Author(s):

J Colby ◽

D I Stirling ◽

H Dalton

Keyword(s):

Aromatic Compounds ◽

Heterocyclic Compounds ◽

Catalytic Properties ◽

Methylococcus Capsulatus ◽

Methylosinus Trichosporium ◽

Styrene Epoxide ◽

Cyclic Alkanes ◽

Methylomonas Albus ◽

Terminal Oxidation ◽

Methylomonas Methanica

1. Methane mono-oxygenase of Methylococcus capsulatus (Bath) catalyses the oxidation of various substituted methane derivatives including methanol. 2. It is a very non-specific oxygenase and, in some of its catalytic properties, apparently resembles the analogous enzyme from Methylomonas methanica but differs from those found in Methylosinus trichosporium and Methylomonas albus. 3. CO is oxidized to CO2. 4. C1-C8 n-alkanes are hydroxylated, yielding mixtures of the corresponding 1- and 2-alcohols; no 3- or 4-alcohols are formed. 5. Terminal alkenes yield the corresponding 1,2-epoxides. cis- or trans-but-2-ene are each oxidized to a mixture of 2,3-epoxybutane and but-2-en-1-ol with retention of the cis or trans configuration in both products; 2-butanone is also formed from cis-but-2-ene only. 6. Dimethyl ether is oxidized. Diethyl ether undergoes sub-terminal oxidation, yielding ethanol and ethanal in equimolar amounts. 7. Methane mono-oxygenase also hydroxylates cyclic alkanes and aromatic compounds. However, styrene yields only styrene epoxide and pyridine yields only pyridine N-oxide. 8. Of those compounds tested, only NADPH can replace NADH as electron donor.

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Faculty Opinions recommendation of UDP-sugar pyrophosphorylase with broad substrate specificity toward various monosaccharide 1-phosphates from pea sprouts.

Faculty Opinions – Post-Publication Peer Review of the Biomedical Literature ◽

10.3410/f.1021628.246636 ◽

2004 ◽

Author(s):

Christoph Benning

Keyword(s):

Substrate Specificity ◽

Broad Substrate Specificity

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Faculty Opinions recommendation of A rice family 9 glycoside hydrolase isozyme with broad substrate specificity for hemicelluloses in type II cell walls.

Faculty Opinions – Post-Publication Peer Review of the Biomedical Literature ◽

10.3410/f.722918335.793513580 ◽

2016 ◽

Author(s):

Daniel Cosgrove

Keyword(s):

Substrate Specificity ◽

Cell Walls ◽

Glycoside Hydrolase ◽

Type Ii ◽

Broad Substrate Specificity ◽

Type Ii Cell

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LASS3 (longevity assurance homologue 3) is a mainly testis-specific (dihydro)ceramide synthase with relatively broad substrate specificity

Biochemical Journal ◽

10.1042/bj20060379 ◽

2006 ◽

Vol 398 (3) ◽

pp. 531-538 ◽

Cited By ~ 116

Author(s):

Yukiko Mizutani ◽

Akio Kihara ◽

Yasuyuki Igarashi

Keyword(s):

Amino Acid ◽

Substrate Specificity ◽

Family Members ◽

Fatty Acyl ◽

Ceramide Synthase ◽

Broad Substrate Specificity ◽

Acid Protein ◽

Amino Acid Protein

The LASS (longevity assurance homologue) family members are highly conserved from yeasts to mammals. Five mouse and human LASS family members, namely LASS1, LASS2, LASS4, LASS5 and LASS6, have been identified and characterized. In the present study we cloned two transcriptional variants of hitherto-uncharacterized mouse LASS3 cDNA, which encode a 384-amino-acid protein (LASS3) and a 419-amino-acid protein (LASS3-long). In vivo, [3H]dihydrosphingosine labelling and electrospray-ionization MS revealed that overproduction of either LASS3 isoform results in increases in several ceramide species, with some preference toward those having middle- to long-chain-fatty acyl-CoAs. A similar substrate preference was observed in an in vitro (dihydro)ceramide synthase assay. These results indicate that LASS3 possesses (dihydro)ceramide synthesis activity with relatively broad substrate specificity. We also found that, except for a weak display in skin, LASS3 mRNA expression is limited almost solely to testis, implying that LASS3 plays an important role in this gland.

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