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  • 1
    ISSN: 1432-2048
    Keywords: Key words: Chloroplast envelope membrane ; Galactosyltransferase ; Sulfolipid ; 16:3/18:3 plants ; Sulfoquinovosyltransferase
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract. In experiments on the assembly of the sulfolipid sulfoquinovosyl diacylglycerol in envelope membranes of chloroplasts, UDP-sulfoquinovose (UDPS) was used with highest efficiency, and the corresponding enzyme, UDP-sulfoquinovose:diacylglycerol sulfoquinovosyltransferase, was partially characterized (E. Heinz et al., 1989, Eur J Biochem 184: 445–453). Here, we identified 35S- and 33P-labelled UDPS from various photosynthetically active organisms, suggesting that the sulfosugar nucleotide used for sulfolipid biosynthesis throughout the plant kingdom, including phototrophic bacteria, may indeed be UDPS. For attribution of the sulfolipid synthase to one of the two plastidial envelope membranes, these membranes were isolated from pea and spinach chloroplasts. The sulfoquinovosyltransferase was localized in the inner membrane of envelopes, which also contains the competing UDP-galactose:diacylglycerol galactosyltransferase. In contrast to the sulfoquinovosyltransferase, a substantial proportion of the galactosyltransferase was found in the outer membranes of envelopes from pea chloroplasts.
    Type of Medium: Electronic Resource
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  • 2
    ISSN: 1617-4623
    Keywords: FadD ; acyl-CoA synthetase ; AMP-binding ; Escherichia coli K12 ; Sequence
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract The fadD gene of Escherichia coli K12 was cloned and sequenced. The gene was identified by its ability to complement the corresponding mutant and by measuring the enzymatic activity after its expression in this mutant. The deduced polypeptide sequence exhibits similarity to other long chain acyl-CoA (coenzyme A) synthetases and a variety of other proteins, which together form a family of AMP-binding proteins. This family is extended by several new members and subdivided into four groups. fadD is assigned to a subgroup that does not include long chain acyl-CoA synthetases from eukaryotic organisms.
    Type of Medium: Electronic Resource
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