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Literature summary for 1.7.6.1 extracted from

  • Varghese, S.; Yang, F.; Pacheco, V.; Wrede, K.; Medvedev, A.; Ogata, H.; Knipp, M.; Heise, H.
    Expression, purification and solid-state NMR characterization of the membrane binding beme protein nitrophorin 7 in two electronic spin states (2013), Biochemistry, 52, 7031-7040.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
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Rhodnius prolixus

Crystallization (Commentary)

Crystallization (Comment) Organism
solid-state NMR analysis. Enzyme tends to form oligomers and precipitates at higher concentration. At concentrations of approximately 0.1-2 mM oligomers are in equilibrium with monomers. The protein oligomerizes preferably in units of trimers, hexamers, and higher oligomeric states of unidentified composition Rhodnius prolixus

Organism

Organism UniProt Comment Textmining
Rhodnius prolixus Q6PQK2
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Subunits

Subunits Comment Organism
More enzyme tends to form oligomers and precipitates at higher concentration. At concentrations of approximately 0.1-2 mM oligomers are in equilibrium with monomers. The protein oligomerizes preferably in units of trimers, hexamers, and higher oligomeric states of unidentified composition Rhodnius prolixus

Synonyms

Synonyms Comment Organism
Nitrophorin 7
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Rhodnius prolixus
NP7
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Rhodnius prolixus