Nomenclature Abstract for Comamonas terrigena (ex Hugh 1962) De Vos et al. 1985 emend. Wauters et al. 2003.

2003 ◽  
Author(s):  
Charles Thomas Parker ◽  
Sarah Wigley ◽  
George M Garrity ◽  
Dorothea Taylor
Keyword(s):  
Comamonas Terrigena

Exemplar Abstract for Comamonas terrigena (ex Hugh 1962) De Vos et al. 1985 emend. Wauters et al. 2003.

2003 ◽  
Author(s):  
Charles Thomas Parker ◽  
Dorothea Taylor ◽  
George M Garrity
Keyword(s):  
Comamonas Terrigena

scholarly journals Comamonas terrigena

2020 ◽  
Author(s):  
Keyword(s):  
Comamonas Terrigena

scholarly journals A novel mechanism of enzymic ester hydrolysis. Inversion of configuration and carbon-oxygen bond cleavage by secondary alkylsulphohydrolases from detergent-degrading micro-organisms

1977 ◽  
Vol 165 (3) ◽  
pp. 575-580 ◽  
Author(s):  
B Bartholomew ◽  
K S Dodgson ◽  
G W J Matcham ◽  
D J Shaw ◽  
G F White
Keyword(s):  
Bond Cleavage ◽  
Hydrolytic Enzymes ◽  
Ester Hydrolysis ◽  
Enzymic Hydrolysis ◽  
Hydrolysis Products ◽  
Bond Scission ◽  
Micro Organisms ◽  
Hydrolysis Of ◽  
Oxygen Bond ◽  
Comamonas Terrigena

The hydrolysis was studied of potassium (+)-octan-2-yl sulphate by two analogous, optically stereospecific, secondary alkylsulphohydrolases purified from two detergent-degrading micro-organisms, Comamonas terrigena and Pseudomonas C12B. Polarimetry studies have shown that (+)-octan-2-yl sulphate prepared from (+)-octan-2-ol is hydrolysed by both enzymes to yield (-)-octan-2-ol. This inversion of configuration implies that the enzymes are catalysing the scission of the C-O bond of the C-O-S linkage, a type of bond scission apparently not hitherto encountered among hydrolytic enzymes acting on ester bonds. Enzymic hydrolysis of potassium (+)-octan-2-yl sulphate in the presence of H218O and analysis of hydrolysis products for the presence of 18O has confirmed that C-O bond scission (and not O-S bond scission) occurs with both enzymes.

scholarly journals Purification, properties and cellular localization of the stereospecific CS2 secondary alkylsulphohydrolase of Comamonas terrigena

1977 ◽  
Vol 167 (3) ◽  
pp. 723-729 ◽  
Author(s):  
G W J Matcham ◽  
K S Dodgson ◽  
J W Fitzgerald
Keyword(s):  
Chain Length ◽  
Cellular Localization ◽  
Indirect Evidence ◽  
Initial Study ◽  
Potassium Salts ◽  
Experimental Conditions ◽  
Alkyl Sulphate ◽  
A Subunit ◽  
A Chain ◽  
Comamonas Terrigena

The availability of homogeneous samples of the potassium salts of L- and D-octan-2-yl sulphate has enabled the separation of the optically stereospecific CS1 and CS2 secondary alkysulphohydrolases from extracts of cells of Comamonas terrigena. The CS2 enzyme was purified to homogeneity, and an initial study was made of its general properties, specificity, cellular localization and relationship to the CS1 enzyme. The CS2 enzyme has a molecular weight of approx. 250000 and a subunit size of approx. 58000, indicating that the molecule is a tetramer. Under the experimental conditions used the enzyme appears to be specific for (+)-secondary alkyl sulphate esters with the sulphate group at C-2 and with a chain length of at least six carbons. Enzyme activity towards racemic C-2 sulphates increases with increasing chain length up to C10, and there is some indirect evidence to suggest that activity declines when that chain length is exceeded. Other indirect evidence confirms that the CS1 enzyme exhibits similar specificity, except that only (-)-isomers can serve as substrates. Both enzymes are present in broth-grown stationary-phase cells of C. terrigena in approximately equal amounts.

scholarly journals The occurrence of an inducible arylsulphatase in Comamonas terrigena

1977 ◽  
Vol 2 (4) ◽  
pp. 221-224 ◽  
Author(s):  
J.W. Fitzgerald ◽  
Marsha E. Cline
Keyword(s):  
Comamonas Terrigena

Expression, purification, and sequence analysis of catalase-1 from the soil bacterium Comamonas terrigena N3H

2004 ◽  
Vol 36 (1) ◽  
pp. 115-123 ◽  
Author(s):  
Marcel Zámocký ◽  
Jana Godočı́ková ◽  
Juraj Gašperı́k ◽  
Franz Koller ◽  
Bystrı́k Polek
Keyword(s):  
Sequence Analysis ◽  
Soil Bacterium ◽  
Comamonas Terrigena

Kinetics of primary biodegradation of sulphosuccinate esters by Comamonas terrigena

1996 ◽  
Vol 37 (3-4) ◽  
pp. 248
Author(s):  
A. Vrbanová ◽  
M. Prokšová ◽  
J. Augustin ◽  
D. Tóth
Keyword(s):  
Kinetics Of ◽  
Comamonas Terrigena

Specificity and other properties of an alcohol dehydrogenase purified from Comamonas terrigena

1981 ◽  
Vol 661 (1) ◽  
pp. 74-86 ◽  
Author(s):  
Carol H. Barrett ◽  
Kenneth S. Dodgson ◽  
Graham F. White
Keyword(s):  
Alcohol Dehydrogenase ◽  
Comamonas Terrigena

scholarly journals Further studies on the substrate specificity and inhibition of the stereospecific CS2 secondary alkylsulphohydrolase of Comamonas terrigena

1980 ◽  
Vol 191 (2) ◽  
pp. 467-473 ◽  
Author(s):  
Carol H. Barrett ◽  
Kenneth S. Dodgson ◽  
Graham F. White
Keyword(s):  
Free Energy ◽  
Chain Length ◽  
Alkyl Chain ◽  
Hydrophobic Interactions ◽  
Standard Free Energy ◽  
Alkyl Chain Length ◽  
Alkyl Sulphate ◽  
Competitive Inhibitors ◽  
Free Energy Of Binding ◽  
Comamonas Terrigena

A series of d-alkan-2-yl sulphate esters (C7–C14) were prepared by sulphation of the resolved parent alcohols by a method that entails complete retention of configuration. These sulphate esters were tested as substrates for the stereospecific CS2 secondary alkylsulphohydrolase of Comamonas terrigena. Vmax. reached a maximum with the C9 compound, whereas logKm decreased linearly as the alkyl-chain length was increased from C7 to C14. A parallel series of l-alkan-2-yl sulphates was also prepared, and these esters, together with homologous series of primary alkyl sulphates and primary alkanesulphonates, were shown to be competitive inhibitors of the CS2 enzyme. For each series of compounds, logKi values decreased linearly with increasing alkyl-chain length. Plots of chain length against the standard free energy of binding (ΔG0) of substrate and inhibitors to the CS2 enzyme showed that the standard free energy of association of a –CH2– group with the enzyme was 2.0–2.4kJ/mol for all classes of compound studied, indicating an important contribution from hydrophobic interactions to the overall binding. Plots for d-alkan-2-yl sulphate substrates and primary alkyl sulphate inhibitors were nearly coincident, suggesting that the overall interaction between a primary ester and the enzyme is the same as that between the isomeric secondary substrate and the enzyme. Plots for l-alkan-2-yl sulphate and alkanesulphonate inhibitors were very similar to each other, but were displaced by 1.5–3.0kJ/mol from that for substrate binding. This indicates that the binding of any one of these particular inhibitors involves one carbon atom fewer than the number involved in binding a substrate of the same chain length. These observations are discussed in terms of a three-point attachment of substrate to the enzyme involving the alkyl chain, sulphate group and the C-1 methyl group.

Sign in / Sign up

Export Citation Format

Share Document