Characterization and crystal structure of lysine insensitive Corynebacterium glutamicum dihydrodipicolinate synthase (cDHDPS) protein

2008 ◽  
Vol 480 (2) ◽  
pp. 111-121 ◽  
Author(s):  
Elena A. Rice ◽  
Gary A. Bannon ◽  
Kevin C. Glenn ◽  
Soon Seog Jeong ◽  
Eric J. Sturman ◽  
...  
2005 ◽  
Vol 62 (1) ◽  
pp. 297-301 ◽  
Author(s):  
Elena Blagova ◽  
Vladimir Levdikov ◽  
Natalia Milioti ◽  
Mark J. Fogg ◽  
Anne K. Kalliomaa ◽  
...  

2014 ◽  
Vol 70 (a1) ◽  
pp. C459-C459
Author(s):  
Kuakarun Krusong ◽  
Wiraya Srisimarat ◽  
Piamsook Pongsawasdi

Amylomaltase (AM; EC 2.4.1.25) belongs to the 4-α-glucanotransferase (4αGTase) group of the α-amylase family. The enzyme can produce cycloamylose (CA) or large-ring cyclodextrin (LR-CD) through intramolecular transglycosylation or cyclization reactions of α-1,4 glucan. Amylomaltase from the mesophilic bacterium Corynebacterium glutamicum yielded different LR-CD production profile from that of the well-characterized Thermus aquaticus enzyme [1,2]. C. glutamicum amylomaltase (CgAM) was overexpressed, purified and crystallized [3]. X-ray crystal structure of CgAM differs from Th. aquaticus amylomaltase in the presence of an additional N-terminus domain. The acarbose- and maltotriose- bound structures revealed the residues involved in substrate binding.


1995 ◽  
Vol 246 (1) ◽  
pp. 227-239 ◽  
Author(s):  
Christian Mirwaldt ◽  
Ingo Korndorfer ◽  
Robert Huber

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