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PMID:8912667

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Citation

Beer, HD, Wohlfahrt, G, Schmid, RD and McCarthy, JE (1996) The folding and activity of the extracellular lipase of Rhizopus oryzae are modulated by a prosequence. Biochem. J. 319 ( Pt 2):351-9

Abstract

The fungus Rhizopus oryzae synthesizes an extracellular lipase precursor bearing N-terminal pre- and pro-sequences. Our studies in Escherichia coli and using recombinant lipase in vitro indicate that the prosequence of 97 amino acids has at least two functions. First, it modulates the enzyme activity of the lipase so that this enzyme can initially be synthesized in a non-destructive form. Direct synthesis of the mature form of the lipase in the cell has toxic consequences, at least partly because of phospholipase activity that is suppressed in the proprotein. Secondly, it supports folding of the lipase via a pathway influenced by a single cysteine residue at position - 68. Mutational analysis of the prosequence demonstrates not only the key role of this cysteine residue but also the importance of the neighbouring amino acids. In particular, Arg-69 probably enhances the leaving group character of Cys-68. We propose a model in which Cys-68 acts as an intramolecular thiodisulphide reagent, playing a catalytic role in the folding of the enzyme. The prosequence is capable of performing the described functions both in cis and in trans.

Links

PubMed PMC1217776

Keywords

Enzyme Activation; Escherichia coli/enzymology; Escherichia coli/genetics; Lipase/chemistry; Lipase/genetics; Lipase/metabolism; Protein Folding; Recombinant Proteins/chemistry; Recombinant Proteins/genetics; Recombinant Proteins/metabolism; Rhizopus/enzymology; Sequence Analysis, DNA

Significance

Annotations

Gene product Qualifier GO Term Evidence Code with/from Aspect Extension Notes Status

RHIOR:B1Q560

GO:0004806: triglyceride lipase activity

ECO:0000314:

F

FIgure 3

complete
CACAO 5354

RHIOR:B1Q560

enables

GO:0004806: triglyceride lipase activity

ECO:0000314: direct assay evidence used in manual assertion

F

Seeded From UniProt

complete


See also

References

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