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Literature summary for 1.7.6.1 extracted from

  • Knipp, M.; Yang, F.; Berry, R.E.; Zhang, H.; Shokhirev, M.N.; Walker, F.A.
    Spectroscopic and functional characterization of nitrophorin 7 from the blood-feeding insect Rhodnius prolixus reveals an important role of its isoform-specific N-terminus for proper protein function (2007), Biochemistry, 46, 13254-13268.
    View publication on PubMedView publication on EuropePMC
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Cloned(Commentary)

Cloned (Comment) Organism
expression in Escherfichia coli Rhodnius prolixus

Protein Variants

Protein Variants Comment Organism
additional information truncated mutant enzyme NP7(DELTA1-3) lacking the 0Met-Leu-Pro-Gly3 sequence, shows marked decay above 45°C. Wild-type nitrophorin 7, in contrast, is comparatively stable, and does not experience a marked signal decrease of activity at temperatures below 52°C Rhodnius prolixus

General Stability

General Stability Organism
the N-terminus of NP7 significantly stabilizes the protein fold Rhodnius prolixus

Organism

Organism UniProt Comment Textmining
Rhodnius prolixus Q6PQK2
-
-

Source Tissue

Source Tissue Comment Organism Textmining
saliva
-
 Rhodnius prolixus
-

Synonyms

Synonyms Comment Organism
Nitrophorin 7
-
 Rhodnius prolixus
NP7
-
 Rhodnius prolixus

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
45
-
 truncated mutant enzyme NP7(DELTA1-3) shows marked decay above 45°C. Wild-type nitrophorin 7, in contrast, is comparatively stable, and does not experience a marked signal decrease of activity at temperatures below 52 °C Rhodnius prolixus
52
-
 truncated mutant enzyme NP7(DELTA1-3) shows marked decay above 45°C. Wild-type nitrophorin 7, in contrast, is comparatively stable, and does not experience a marked signal decrease of activity at temperatures below 52 °C Rhodnius prolixus

Cofactor

Cofactor Comment Organism Structure
heme nitrophorin 7 strongly favors the A orientation of the heme Rhodnius prolixus