Structure and mechanism of the Propionibacterium acnes polyunsaturated fatty acid isomerase.

Abstract:

:Conjugated linoleic acids (CLAs) affect body fat gain, carcinogenesis, insulin resistance, and lipid peroxidation in mammals. Several isomers of CLA exist, of which the (9Z, 11E) and (10E, 12Z) isomers have beneficial effects on human metabolism but are scarce in foods. Bacterial polyunsaturated fatty acid isomerases are promising biotechnological catalysts for CLA production. We describe six crystal structures of the Propionibacterium acnes polyunsaturated fatty acid isomerase PAI in apo- and product-bound forms. The three-domain flavoprotein has previously undescribed folds outside the FAD-binding site. Conformational changes in a hydrophobic channel toward the active site reveal a unique gating mechanism for substrate specificity. The geometry of the substrate-binding site explains the length preferences for C18 fatty acids. A catalytic mechanism for double-bond isomerization is formulated that may be altered to change substrate specificity for syntheses of rare CLAs from easily accessible precursors.

authors

Liavonchanka A,Hornung E,Feussner I,Rudolph MG

doi

10.1073/pnas.0510144103

keywords:

subject

Has Abstract

pub_date

2006-02-21 00:00:00

pages

2576-81

issue

8

eissn

0027-8424

issn

1091-6490

pii

0510144103

journal_volume

103

pub_type

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