Refined Crystal Structure of the Catalytic Domain of Dihydrolipoyl Transacetylase (E2p) from Azotobacter vinelandii at 2·6 Å Resolution

Mattevi, Andrea; Obmolova, G.; Kalk, Kor H.; Westphal, Adrie H.; Kok, A. de; Hol, W.G.J.

doi:10.1006/jmbi.1993.1235

Cited by 63 publications

(66 citation statements)

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“…1a), with the internal interactions between monomers being essentially the same as in other reported E2 CD trimers (15,(17)(18)(19)(20)(21)(22)(23)(24)(25). Each E2pCD subunit consists of a V-shaped N-terminal arm (residues 381-407) and a main globular portion (residues 408 -629).…”

Section: Overall Description Of the E2pcd X-ray Structure-threesupporting

confidence: 70%

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Structure and Function of the Catalytic Domain of the Dihydrolipoyl Acetyltransferase Component in Escherichia coli Pyruvate Dehydrogenase Complex

Wang

Nemeria

Chandrasekhar

et al. 2014

Journal of Biological Chemistry

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Background: The E. coli pyruvate dehydrogenase complex catalyzes conversion of pyruvate to acetyl-CoA and comprises E1p, E2p, and E3 components. Results: The structure of the E2 core domain was solved and shown to efficiently catalyze acetyl transfer between domains. Conclusion: Mass spectrometry revealed hitherto unrecognized domain-induced interactions between E1 and E2 core domain. Significance: A multifaceted approach is required to understand communication between intact multidomain components.

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Section: Overall Description Of the E2pcd X-ray Structure-threesupporting

confidence: 70%

“…Although the structure of E2CDs from different sources has been reported (15,(17)(18)(19)(20)(21)(22)(23)(24)(25), we here present the x-ray structure of the E2pCD from E. coli and its functions.…”

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confidence: 99%

Structure and Function of the Catalytic Domain of the Dihydrolipoyl Acetyltransferase Component in Escherichia coli Pyruvate Dehydrogenase Complex

Wang

Nemeria

Chandrasekhar

et al. 2014

Journal of Biological Chemistry

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“…Preliminary analysis reveals that PapA5 is a pseudodimer of two CAT domains, a property also observed in the stand-alone CD VibH (34). The N-terminal 150 residues of PapA5 share a high degree of structural alignment to CAT, dihydrolipoamide acetyltransferase (E2p) (43), and VibH, particularly with respect to the Hx 3 D motif conserved residues. Consistent with Papa5 activities on model substrates, we also observed a deep hydrophobic channel that links the Papa5 surface to the proposed active site.…”

Section: Discussionmentioning

confidence: 80%

Mycobacterial polyketide-associated proteins are acyltransferases: Proof of principle with Mycobacterium tuberculosis PapA5

Onwueme

Ferreras

Buglino

et al. 2004

Proc. Natl. Acad. Sci. U.S.A.

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Mycobacterium tuberculosis (Mt) produces complex virulence-enhancing lipids with scaffolds consisting of phthiocerol and phthiodiolone dimycocerosate esters (PDIMs). Sequence analysis suggested that PapA5, a so-called polyketide-associated protein (Pap) encoded in the PDIM synthesis gene cluster, as well as PapA5 homologs found in Mt and other species, are a subfamily of acyltransferases. Studies with recombinant protein confirmed that PapA5 is an acetyltransferase. Deletion analysis in Mt demonstrated that papA5 is required for PDIM synthesis. We propose that PapA5 catalyzes diesterification of phthiocerol and phthiodiolone with mycocerosate. These studies present the functional characterization of a Pap and permit inferences regarding roles of other Paps in the synthesis of complex lipids, including the antibiotic rifamycin

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“…After the oxidized E2-bound lipoyl moiety has left its E3 binding site, free lipoate from the medium Dihydrolipoyl acetyltransferase of the pyruvate dehydrogenase complex shows also stereoselectivity for R-lipoate [8,14]. However, this enzyme cannot execute the reduction of lipoate, since the formation of the two electron-reduced enzyme in this case is not possible and each active site of E2 contains only one binding site for the lipoate moiety [15,16]. This argues against the assumption that Reaction 4 may proceed in the active center of E2.…”

Section: Discussionmentioning

confidence: 99%

Using lipoate enantiomers and thioredoxin to study the mechanism of the 2‐oxoacid‐dependent dihydrolipoate production by the 2‐oxoacid dehydrogenase complexes

et al. 1995

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The thioredoxin-catalyzed insulin reduction by dihydrolipoate was applied to study the 2-oxoacid:lipoate oxidoreductase activity of 2-oxoacid dehydrogenase complexes. The enzymatic and non-enzymatic mechanisms of the transfer of reducing equivalents from the complexes to free lipoic acid (a-lipoic acid, 6,8-thiooctic acid) were distinguished using the high stereoselectivity of the complex enzymes to the R-enantiomer of lipoate. Unlike these enzymes, thioredoxin from E. coli exibited no stereoselectivity upon reduction with chemically obtained dihydrolipoate. However, coupled to the dihydrolipoate production by the dehydrogenase complexes, the process was essentially sensitive both to the enantiomer used and the dihydrolipoyl dehydrogenase activity of the complexes. These results indicated the involvement of the third complex component, dihydrolipoyl dehydrogenase, in the 2-oxoacid-dependent dihydrolipoate formation. The implication of the investigated reaction for a connection between thioredoxin and the 2-oxoacid dehydrogenase complexes in the mitochondrial metabolism are discussed.

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Refined Crystal Structure of the Catalytic Domain of Dihydrolipoyl Transacetylase (E2p) from Azotobacter vinelandii at 2·6 Å Resolution

Cited by 63 publications

References 0 publications

Structure and Function of the Catalytic Domain of the Dihydrolipoyl Acetyltransferase Component in Escherichia coli Pyruvate Dehydrogenase Complex

Structure and Function of the Catalytic Domain of the Dihydrolipoyl Acetyltransferase Component in Escherichia coli Pyruvate Dehydrogenase Complex

Mycobacterial polyketide-associated proteins are acyltransferases: Proof of principle with Mycobacterium tuberculosis PapA5

Using lipoate enantiomers and thioredoxin to study the mechanism of the 2‐oxoacid‐dependent dihydrolipoate production by the 2‐oxoacid dehydrogenase complexes

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