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| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
2
|
| pubmed:dateCreated |
1990-9-11
|
| pubmed:abstractText |
NADH peroxidase (EC 1.11.1.1) previously isolated from Streptococcus faecalis 10C1 has been crystallized. The crystal structure has been solved by multiple isomorphous replacement and solvent-flattening at 3.3 A (1 A = 0.1 nm) resolution. The enzyme forms a tetramer consisting of 4 crystallographically related subunits. The monomer chain fold is in general similar to those of glutathione reductase and lipoamide dehydrogenase. FAD binds in the same region and in a similar conformation as in glutathione reductase. The unusual cysteine-sulfenic acid participating in catalysis is located at the isoalloxazine of FAD.
|
| pubmed:grant | |
| pubmed:language |
eng
|
| pubmed:journal | |
| pubmed:citationSubset |
IM
|
| pubmed:chemical | |
| pubmed:status |
MEDLINE
|
| pubmed:month |
Jul
|
| pubmed:issn |
0014-5793
|
| pubmed:author | |
| pubmed:issnType |
Print
|
| pubmed:day |
16
|
| pubmed:volume |
267
|
| pubmed:owner |
NLM
|
| pubmed:authorsComplete |
Y
|
| pubmed:pagination |
186-8
|
| pubmed:dateRevised |
2007-11-14
|
| pubmed:meshHeading |
pubmed-meshheading:2116319-Crystallization,
pubmed-meshheading:2116319-Cysteine,
pubmed-meshheading:2116319-Enterococcus faecalis,
pubmed-meshheading:2116319-Flavin-Adenine Dinucleotide,
pubmed-meshheading:2116319-Models, Molecular,
pubmed-meshheading:2116319-Peroxidases,
pubmed-meshheading:2116319-Protein Conformation,
pubmed-meshheading:2116319-X-Ray Diffraction
|
| pubmed:year |
1990
|
| pubmed:articleTitle |
The structure of NADH peroxidase from Streptococcus faecalis at 3.3 A resolution.
|
| pubmed:affiliation |
Institut für Organische Chemie und Biochemie, Freiburg, FRG.
|
| pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, Non-U.S. Gov't
|