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Titolo:
Lipoamide dehydrogenase from Corynebacterium glutamicum: molecular and physiological analysis of the lpd gene and characterization of the enzyme
Autore:
Schwinde, JW; Hertz, PF; Sahm, H; Eikmanns, BJ; Guyonvarch, A;
Indirizzi:
Univ Paris 11, Inst Genet & Microbiol, Ctr Orsay, F-91405 Orsay, France Univ Paris 11 Orsay France F-91405 iol, Ctr Orsay, F-91405 Orsay, France KFA Julich GmbH, Forschungszentrum, Inst Biotechnol, D-52425 Julich, Germany KFA Julich GmbH Julich Germany D-52425 otechnol, D-52425 Julich, Germany
Titolo Testata:
MICROBIOLOGY-SGM
, volume: 147, anno: 2001,
parte:, 8
pagine: 2223 - 2231
SICI:
1350-0872(200108)147:<2223:LDFCGM>2.0.ZU;2-L
Fonte:
ISI
Lingua:
ENG
Soggetto:
MITOCHONDRIAL NADH->NAD TRANSHYDROGENATION; ADULT HYMENOLEPIS-DIMINUTA; PYRUVATE-DEHYDROGENASE; ESCHERICHIA-COLI; SEQUENCE-ANALYSIS; NUCLEOTIDE-SEQUENCE; 2-OXOGLUTARATE DEHYDROGENASE; CLONING; COMPLEX; IDENTIFICATION;
Keywords:
Corynebacterium glutamicum; lpd gene; initiation of transcription; initiation of translation;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
44
Recensione:
Indirizzi per estratti:
Indirizzo: Guyonvarch, A Univ Paris 11, Inst Genet & Microbiol, Ctr Orsay, Bat 360, F-91405 Orsay, France Univ Paris 11 Bat 360 Orsay France F-91405 05 Orsay, France
Citazione:
J.W. Schwinde et al., "Lipoamide dehydrogenase from Corynebacterium glutamicum: molecular and physiological analysis of the lpd gene and characterization of the enzyme", MICROBI-SGM, 147, 2001, pp. 2223-2231

Abstract

Lipoamide dehydrogenase (LPD) is an essential component of the pyruvate dehydrogenase and 2-oxoglutarate dehydrogenase complexes, both playing a crucial role within the central metabolism of aerobic organisms. Using oligonucleotides designed according to conserved regions of LPD amino acid sequences from several organisms, the Ipd gene from Corynebacterium glutamicum was identified and subsequently subcloned. The cloned Ipd gene expressed in C. glutamicum cells harbouring the gene on a plasmid showed a 12-fold higher specific LPD activity when compared to the wild-type strain. DNA sequence analysis of a 4524 bp segment containing the Ipd gene and adjacent regions revealed that the Ipd gene is not flanked by genes encoding other subunits ofthe pyruvate or 2-oxoglutarate dehydrogenase complexes and predicted an LPD polypeptide of 469 amino acids with an M-r of 50619. The amino acid sequence of this polypeptide shows between 26 and 58 % identity when compared toLPD enzymes from other organisms. Transcriptional analyses revealed that the Ipd gene from C. glutamicum is monocistronic (1(.)45 kb mRNA) and that its transcription is initiated exactly at the nucleotide defined as the translational start. LPD was purified and biochemically characterized. This analysis revealed that the enzyme catalyses the reversible reoxidation of dihydrolipoic acid and NADH:NAD(+) transhydrogenation, and is able to transfer electrons from NADH to various redox-active compounds and quinones. An in vivo participation of C. glutamicum LPD in facilitation of quinone redox cycling is proposed.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 16/07/20 alle ore 19:53:05