Please use this identifier to cite or link to this item:
Title: Archaeal proline dehydrogenase from Pyrobaculum aerophilum : sequence comparison.
Authors: Kik, Shian Chi.
Keywords: DRNTU::Engineering::Chemical engineering::Biotechnology
Issue Date: 2009
Abstract: Based on the amino acid sequence, proline dehydrogenase from hyperthermophilic archaeon, Pyrobaculum aerophilum showed no significant homology with previously known bacterial proline dehydrogenase, as exemplified with Salmonella typhimurium and Escherichia Coli putA proteins, as well as archaeal dye-linked L-proline dehydrogenase from Thermococcus profundus. Multiple sequence alignment revealed a close relation to the archaeal FAD dependent oxidoreductase enzyme family. Gene organizations around Pyrobaculum aerophilum proline dehydrogenase and archaeal FAD dependent oxidoreductases were similar, suggesting possibly similar amino acid regulation and catabolism. However, differences were recorded in the stereospecificity of amino acid activity. The predicted model of Pyrobaculum aerophilum proline dehydrogenase demonstrated high structural similarity to sarcosine oxidase from Corynebacterium sp. U-96 and L-proline dehydrogenase from Pyrococcus horikoshii with root mean square deviation of 2.043 and 1.983 respectively. Nonetheless, low amino acid sequence homology categorizes the Pyrobaculum aerophilum enzyme as an independent class of enzymes.
Rights: Nanyang Technological University
Fulltext Permission: restricted
Fulltext Availability: With Fulltext
Appears in Collections:SCBE Student Reports (FYP/IA/PA/PI)

Files in This Item:
File Description SizeFormat 
  Restricted Access
7.44 MBAdobe PDFView/Open

Page view(s)

Updated on Jan 18, 2021


Updated on Jan 18, 2021

Google ScholarTM


Items in DR-NTU are protected by copyright, with all rights reserved, unless otherwise indicated.