N-lipoyl glucosamine and N-lipoyl glucosaminitol: Substrates for lipoyl dehydrogenase

Fluharty, Aryan L.; Adelson, Gary L.; Gaber, Bruce P.

doi:10.1016/0003-9861(69)90293-8

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1972

1973

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Cited by 3 publications

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“…It may also be significant, in so far as knowledge of this extended portion of primary structure allows one to judge, that the active site of lipoamide dehydrogenase appears to be relatively apolar [13]. This would be in keeping with its substrate, enzyme-bound lipoic acid [17].…”

Section: Discussionmentioning

confidence: 99%

An amino acid sequence in the active site of lipoamide dehydrogenase from the 2‐oxoglutarate dehydrogenase complex ofE. coli (Crookes strain)

Brown

Perham

1972

FEBS Letters

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Section: Discussionmentioning

confidence: 99%

An amino acid sequence in the active site of lipoamide dehydrogenase from the 2‐oxoglutarate dehydrogenase complex ofE. coli (Crookes strain)

Brown

Perham

1972

FEBS Letters

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Cadmium and arsenite binding byN-dihydrolipoyl-aminoethoxydextran: A model study of enzyme dithiol criteria

Gaber

Fluharty

1973

Bioinorganic Chemistry

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We have observed the interaction of Cd=+, Zi+, and AsOz* with a dithiolsubstituted polymer (N-diiydrolipoyl aminoethoq dextran). Cadmium binding results in an intense uv difference spectrum (x, = 249 nm). Spectrophotometric titrations with CdCl: roves1 formation of two Cd-dithiol complexes characterized as 2-SH/Cd*+ and 3SH/Cd*+. Stability constants were determined by titration of cadmium-saturated polymer with es& EDT.... For the two complexes, KI = 2.7 X 1014 Jf and R= = 7.7 X lOI3 M_ NT-4 is not effective in d&placing Cd?+_ In competition of Cd?* snd Znt+ for dithiol sites, Cd*+ is bound about 599 times more firmly than Zn*f_ Arsenite binding is siuggish (K-85 M-' see-I) and yields a single complex (2-SH/AsO*'-). Competition and kinetic data suggest that 106 Jf < K&e-< lo" M. We have defined basic criteria for evaluation of enzyme active-site &hiols: (1) the binding order "cadium stronger than zinc"; (2) relief of Cd%+ inhibition by l9-fold ezeess EDTh and no relief by lo-fold excess of NTA; (3) inhibition by arsenite.

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The Isolation and Primary Structure of a Peptide Containing the Oxidation-Reduction Active Cystine of Escherichia coli Lipoamide Dehydrogenase

Burleigh

Williams

1972

Journal of Biological Chemistry

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N-lipoyl glucosamine and N-lipoyl glucosaminitol: Substrates for lipoyl dehydrogenase

Cited by 3 publications

References 7 publications

An amino acid sequence in the active site of lipoamide dehydrogenase from the 2‐oxoglutarate dehydrogenase complex ofE. coli (Crookes strain)

An amino acid sequence in the active site of lipoamide dehydrogenase from the 2‐oxoglutarate dehydrogenase complex ofE. coli (Crookes strain)

Cadmium and arsenite binding byN-dihydrolipoyl-aminoethoxydextran: A model study of enzyme dithiol criteria

The Isolation and Primary Structure of a Peptide Containing the Oxidation-Reduction Active Cystine of Escherichia coli Lipoamide Dehydrogenase

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