Synapse
⌘+K
Synapse
PulseExploreClubsResearchersJournals
Instagram
HomeClubsExplore
January 1, 1996Biochemistry

Identification of Glutamic Acid 381 as a Candidate Active Site Residue of Pseudomonas aeruginosa Exoenzyme S

View Full Paper
Ask AI
Bookmark
Share

Authors

SLSuyan LiuFujian University of Traditional Chinese MedicineSKScott KulichUniversity of PittsburghJBJoseph BarbieriMedical College of Wisconsin

Discussion

Loading...

Member takes

Implication

Key Points

Key points are not available for this paper at this time.

Cite This Study

Liu et al. (1996) studied this question.

synapsesocial.com/papers/6a9ec295596cbcc64e8c4dfbhttps://doi.org/10.1021/bi952340g
View Full Paper
Ask AI
Bookmark
Share

Also Consider

Synapse has enriched 5 closely related papers on similar clinical questions. Consider them for comparative context:

  1. 1Evidence for a catalytic role of glutamic acid 129 in the NAD-glycohydrolase activity of the pertussis toxin S1 subunit.1993 · 40 citations
  2. 2The NAD-glycohydrolase activity of the pertussis toxin S1 subunit. Involvement of the catalytic HIS-35 residue.1994 · 35 citations
  3. 3Several GTP-binding Proteins, Including p21c-H-ras, Are Preferred Substrates of Pseudomonas aeruginosa Exoenzyme S1989 · 126 citations
  4. 4Expression of recombinant exoenzyme S of Pseudomonas aeruginosa1995 · 58 citations
  5. 5Cloning the structural gene for the 49-kDa form of exoenzyme S (exoS) from Pseudomonas aeruginosa strain 388.1994 · 93 citations