Bacterial utilisation of short-chain primary alkyl sulphate esters

White, Gail L.

doi:10.1016/0378-1097(87)90371-5

“…The ability of MSAMO to desul-fonate only short-chain sulfonates suggests that metabolism of primary aliphatic sulfonates by different enzymes may be carbon-chain-length-dependent. Interestingly, biodegradation of a similar group of compounds, the primary alkyl sulfates, show similar patterns (Cloves et al ., 1980; Bateman et al ., 1986; White et al ., 1987; Higgins et al ., 1993; Matts et al ., 1994). The existence of distinct enzymes for the degradation of short-, medium- and long-chain alkyl sulfates is thought to be due to the hydrophobic contributions of the alkyl chains to enzyme-substrate interactions (Matts et al ., 1994).…”

Section: Discussionmentioning

confidence: 99%

Metabolism of methanesulfonic acid involves a multicomponent monooxygenase enzyme

Higgins

¹

,

Davey

²

,

Trickett³

et al. 1996

View full text Add to dashboard Cite

A novel methylotroph, strain M2, capable of utilizing methanesulfonic acid (MSA) as a sole source of carbon and energy was the subject of these investigations. The initial step in the biodegradative pathway of MSA in strain LL, UK M2 involved an inducible NADH-specif ic monooxygenase enzyme (MSAMO). Partial purification of MSAMO from cell-free extracts by ion-exchange chromatography led to the loss of MSAMO activity. Activity was restored by the mixing of three distinct protein fractions designated A, B and C. The reconstituted enzyme had a narrow substrate specificity relative to crude cellfree extracts. Addition of FAD and ferrous ions to the reconstituted enzyme complex resulted in a fivefold increase in enzyme activity, suggesting the loss of FAD and ferrous ion from the multicomponent enzyme on purification. Analysis of mutants of strain M2 defective in the metabolism of C, compounds indicated that methanol was not an intermediate in the degradative pathway of MSA and also confirmed the involvement of a multicomponent enzyme in the degradation of MSA by methylotroph strain M2.

show abstract

“…Studies with the Pseudomonas C 12 B alkylsulfatases revealed that these were speci¢c for medium-or long-chain sulfate esters, but had little or no activity with substrates with a chain length less than C 5 . However, organisms have subsequently been isolated from soil, canal water and sewage which are able to grow with short-chain alkylsulfates as carbon source [157], and several of these have been examined in more detail. The sulfatase of the coryneform isolate B1A was active on C 3^C7 primary alkylsulfates, but not on longer or shorter-chain homologues, nor on choline sulfate [152].…”

Section: Alkylsulfatasesmentioning

confidence: 99%

Riding the sulfur cycle – metabolism of sulfonates and sulfate esters in Gram-negative bacteria

Kertesz

¹

2000

View full text Add to dashboard Cite

Sulfonates and sulfate esters are widespread in nature, and make up over 95% of the sulfur content of most aerobic soils. Many microorganisms can use sulfonates and sulfate esters as a source of sulfur for growth, even when they are unable to metabolize the carbon skeleton of the compounds. In these organisms, expression of sulfatases and sulfonatases is repressed in the presence of sulfate, in a process mediated by the LysR-type regulator protein CysB, and the corresponding genes therefore constitute an extension of the cys regulon. Additional regulator proteins required for sulfonate desulfonation have been identified in Escherichia coli (the Cbl protein) and Pseudomonas putida (the AsfR protein). Desulfonation of aromatic and aliphatic sulfonates as sulfur sources by aerobic bacteria is oxygendependent, carried out by the K-ketoglutarate-dependent taurine dioxygenase, or by one of several FMNH 2 -dependent monooxygenases. Desulfurization of condensed thiophenes is also FMNH 2 -dependent, both in the rhodococci and in two Gram-negative species. Bacterial utilization of aromatic sulfate esters is catalyzed by arylsulfatases, most of which are related to human lysosomal sulfatases and contain an active-site formylglycine group that is generated post-translationally. Sulfate-regulated alkylsulfatases, by contrast, are less well characterized. Our increasing knowledge of the sulfur-regulated metabolism of organosulfur compounds suggests applications in practical fields such as biodesulfurization, bioremediation, and optimization of crop sulfur nutrition. ß

show abstract

“…Studies with the Pseudomonas C 12 B alkylsulfatases revealed that these were specific for medium‐ or long‐chain sulfate esters, but had little or no activity with substrates with a chain length less than C 5 . However, organisms have subsequently been isolated from soil, canal water and sewage which are able to grow with short‐chain alkylsulfates as carbon source [157], and several of these have been examined in more detail. The sulfatase of the coryneform isolate B1A was active on C 3 –C 7 primary alkylsulfates, but not on longer or shorter‐chain homologues, nor on choline sulfate [152].…”

Section: Sulfatases – From Bacteria To Humansmentioning

confidence: 99%

Riding the sulfur cycle â metabolism of sulfonates and sulfate esters in Gram-negative bacteria

Kertesz

¹

2000

FEMS Microbiology Reviews

View full text Add to dashboard Cite

Sulfonates and sulfate esters are widespread in nature, and make up over 95% of the sulfur content of most aerobic soils. Many microorganisms can use sulfonates and sulfate esters as a source of sulfur for growth, even when they are unable to metabolize the carbon skeleton of the compounds. In these organisms, expression of sulfatases and sulfonatases is repressed in the presence of sulfate, in a process mediated by the LysR-type regulator protein CysB, and the corresponding genes therefore constitute an extension of the cys regulon. Additional regulator proteins required for sulfonate desulfonation have been identified in Escherichia coli (the Cbl protein) and Pseudomonas putida (the AsfR protein). Desulfonation of aromatic and aliphatic sulfonates as sulfur sources by aerobic bacteria is oxygendependent, carried out by the K-ketoglutarate-dependent taurine dioxygenase, or by one of several FMNH 2 -dependent monooxygenases. Desulfurization of condensed thiophenes is also FMNH 2 -dependent, both in the rhodococci and in two Gram-negative species. Bacterial utilization of aromatic sulfate esters is catalyzed by arylsulfatases, most of which are related to human lysosomal sulfatases and contain an active-site formylglycine group that is generated post-translationally. Sulfate-regulated alkylsulfatases, by contrast, are less well characterized. Our increasing knowledge of the sulfur-regulated metabolism of organosulfur compounds suggests applications in practical fields such as biodesulfurization, bioremediation, and optimization of crop sulfur nutrition. ß

show abstract

Bacterial utilisation of short-chain primary alkyl sulphate esters

Cited by 4 publications

References 2 publications

Metabolism of methanesulfonic acid involves a multicomponent monooxygenase enzyme

Metabolism of methanesulfonic acid involves a multicomponent monooxygenase enzyme

Riding the sulfur cycle – metabolism of sulfonates and sulfate esters in Gram-negative bacteria

Riding the sulfur cycle â metabolism of sulfonates and sulfate esters in Gram-negative bacteria

Contact Info

Product

Resources

About

Bacterial utilisation of short-chain primary alkyl sulphate esters

Cited by 4 publications

References 2 publications

Metabolism of methanesulfonic acid involves a multicomponent monooxygenase enzyme

Metabolism of methanesulfonic acid involves a multicomponent monooxygenase enzyme

Riding the sulfur cycle – metabolism of sulfonates and sulfate esters in Gram-negative bacteria

Riding the sulfur cycle â metabolism of sulfonates and sulfate esters in Gram-negative bacteria

Contact Info

Product

Resources

About

Riding the sulfur cycle â metabolism of sulfonates and sulfate esters in Gram-negative bacteria