Structural classification and properties of ketoacyl reductases, hydroxyacyl dehydratases and enoyl reductases.

نویسندگان

  • David C Cantu
  • Tingsong Dai
  • Zachary S Beversdorf
  • Peter J Reilly
چکیده

Ketoacyl reductases (KRs), hydroxyacyl dehydratases (HDs) and enoyl reductases (ERs) are part of the fatty acid and polyketide synthesis cycles. Their reverse reactions, catalyzed by acyl dehydrogenases (equivalent to ERs), enoyl hydratases (equivalent to HDs) and hydroxyacyl dehydrogenases (equivalent to KRs), are part of fatty acid degradation by β-oxidation. These enzymes have been classified into families based on similarities in their primary and tertiary structures, and these families and their structures are included in the ThYme (Thioester-active enzYmes) database. Members of each family have strong sequence similarity and have essentially the same tertiary structure, mechanism and catalytic residues.

برای دانلود متن کامل این مقاله و بیش از 32 میلیون مقاله دیگر ابتدا ثبت نام کنید

ثبت نام

اگر عضو سایت هستید لطفا وارد حساب کاربری خود شوید

منابع مشابه

Crystal structure of hexanoyl-CoA bound to β-ketoacyl reductase FabG4 of Mycobacterium tuberculosis.

FabGs, or β-oxoacyl reductases, are involved in fatty acid synthesis. The reaction entails NADPH/NADH-mediated conversion of β-oxoacyl-ACP (acyl-carrier protein) into β-hydroxyacyl-ACP. HMwFabGs (high-molecular-weight FabG) form a phylogenetically separate group of FabG enzymes. FabG4, an HMwFabG from Mycobacterium tuberculosis, contains two distinct domains, an N-terminal 'flavodoxintype' doma...

متن کامل

The large subunit of the fatty acid oxidation complex from Escherichia coli is a multifunctional polypeptide. Evidence for the existence of a fatty acid oxidation operon (fad AB) in Escherichia coli.

The subunit locations of the five enzymes associated with the fatty acid oxidation complex from Escherichia coli were studied by immunotitration and chemical modification. Antibodies raised against the purified complex caused the parallel inhibitions of enoyl-CoA hydratase and 3-hydroxyacyl-CoA dehydrogenase, while slightly stimulating 3-ketoacyl-CoA thiolase. All five component enzymes of the ...

متن کامل

The Large Subunit of the Fatty Acid Oxidation Complex from Escherichia coli Is a Multifunctional Polypeptide

The subunit locations of the five enzymes associated with the fatty acid oxidation complex from Escherichia coli were studied by immunotitration and chemical modification. Antibodies raised against the purified complex caused the parallel inhibitions of enoyl-CoA hydratase and 3-hydroxyacyl-CoA dehydrogenase, while slightly stimulating 3-ketoacyl-CoA thiolase. All five component enzymes of t...

متن کامل

Members of the Arabidopsis FAE1-like 3-ketoacyl-CoA synthase gene family substitute for the Elop proteins of Saccharomyces cerevisiae.

Several 3-keto-synthases have been studied, including the soluble fatty acid synthases, those involved in polyketide synthesis, and the FAE1-like 3-ketoacyl-CoA synthases. All of these condensing enzymes have a common ancestor and an enzymatic mechanism that involves a catalytic triad consisting of Cys, His, and His/Asn. In contrast to the FAE1-like family of enzymes that mediate plant microsom...

متن کامل

Carboxylation mechanism and stereochemistry of crotonyl-CoA carboxylase/reductase, a carboxylating enoyl-thioester reductase.

Chemo- and stereoselective reductions are important reactions in chemistry and biology, and reductases from biological sources are increasingly applied in organic synthesis. In contrast, carboxylases are used only sporadically. We recently described crotonyl-CoA carboxylase/reductase, which catalyzes the reduction of (E)-crotonyl-CoA to butyryl-CoA but also the reductive carboxylation of (E)-cr...

متن کامل

ذخیره در منابع من


  با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید

برای دانلود متن کامل این مقاله و بیش از 32 میلیون مقاله دیگر ابتدا ثبت نام کنید

ثبت نام

اگر عضو سایت هستید لطفا وارد حساب کاربری خود شوید

عنوان ژورنال:
  • Protein engineering, design & selection : PEDS

دوره 25 12  شماره 

صفحات  -

تاریخ انتشار 2012