PMID:1995341: Difference between revisions

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<span style = 'font-size: large'> '''McKie, JH and Douglas, KT'''  (1991) Evidence for gene duplication forming similar binding folds for NAD(P)H and FAD in pyridine nucleotide-dependent flavoenzymes.''FEBS Lett.'' '''279''':5-8</span>
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!align=left  |Citation
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'''No author listed'''  (1991) Evidence for gene duplication forming similar binding folds for NAD(P)H and FAD in pyridine nucleotide-dependent flavoenzymes. ''FEBS Lett.'' '''279''':5-8
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!align=left  |Abstract
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For pyridine nucleotide-dependent flavoenzymes, binding both FAD and NAD(P)H on a single amino-acid chain, we have found a high degree of internal sequence similarity for certain regions of the FAD and NAD(P)H binding portions of the chain for any given protein. This was the case for a range of enzyme classes, including disulphide oxidoreductases (such as glutathione reductase, trypanothione reductase, lipoamide dehydrogenase, mercuric reductase), mono- and dioxygenases, nitrite reductase, alkyl hydroperoxidase and NADH dehydrogenase from E. coli. This provides strong support for gene duplication as the origin of at least part of the FAD and NAD(P)H recognising domains of such enzymes.
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[http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=1995341 PubMed]


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|{{TableHeadingColor}} |'''Abstract''' || For pyridine nucleotide-dependent flavoenzymes, binding both FAD and NAD(P)H on a single amino-acid chain, we have found a high degree of internal sequence similarity for certain regions of the FAD and NAD(P)H binding portions of the chain for any given protein. This was the case for a range of enzyme classes, including disulphide oxidoreductases (such as glutathione reductase, trypanothione reductase, lipoamide dehydrogenase, mercuric reductase), mono- and dioxygenases, nitrite reductase, alkyl hydroperoxidase and NADH dehydrogenase from E. coli. This provides strong support for gene duplication as the origin of at least part of the FAD and NAD(P)H recognising domains of such enzymes.
!align=left  |Keywords
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Amino Acid Sequence; Animals; Bacteria/enzymology; Binding Sites; Escherichia coli/enzymology; Flavin-Adenine Dinucleotide/genetics; Humans; Models, Molecular; Molecular Sequence Data; Multigene Family; NADP/genetics; Oxidoreductases/genetics; Sequence Homology, Nucleic Acid; Swine
|{{TableHeadingColor}} nowrap |'''Links''' ||  [http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=1995341 PubMed]
 
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==Significance {{HelpIcon|Help:Literature}} ==
==Significance {{HelpIcon|Help:Literature}} ==
{{LitSignificance}}
{{LitSignificance}}

Revision as of 19:08, 1 September 2013

Citation

No author listed (1991) Evidence for gene duplication forming similar binding folds for NAD(P)H and FAD in pyridine nucleotide-dependent flavoenzymes. FEBS Lett. 279:5-8

Abstract

For pyridine nucleotide-dependent flavoenzymes, binding both FAD and NAD(P)H on a single amino-acid chain, we have found a high degree of internal sequence similarity for certain regions of the FAD and NAD(P)H binding portions of the chain for any given protein. This was the case for a range of enzyme classes, including disulphide oxidoreductases (such as glutathione reductase, trypanothione reductase, lipoamide dehydrogenase, mercuric reductase), mono- and dioxygenases, nitrite reductase, alkyl hydroperoxidase and NADH dehydrogenase from E. coli. This provides strong support for gene duplication as the origin of at least part of the FAD and NAD(P)H recognising domains of such enzymes.

Links

PubMed

Keywords

Amino Acid Sequence; Animals; Bacteria/enzymology; Binding Sites; Escherichia coli/enzymology; Flavin-Adenine Dinucleotide/genetics; Humans; Models, Molecular; Molecular Sequence Data; Multigene Family; NADP/genetics; Oxidoreductases/genetics; Sequence Homology, Nucleic Acid; Swine

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