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Inside Cover: Structural and Mutational Studies on the Unusual Substrate Specificity of meso ‐Diaminopimelate Dehydrogenase from Symbiobacterium thermophilum (ChemBioChem 2/2014)
Author(s) -
Liu Weidong,
Li Zhe,
Huang ChunHsiang,
Guo ReyTing,
Zhao Leiming,
Zhang Dalong,
Chen Xi,
Wu Qiaqing,
Zhu Dunming
Publication year - 2014
Publication title -
chembiochem
Language(s) - English
Resource type - Reports
SCImago Journal Rank - 1.05
H-Index - 126
eISSN - 1439-7633
pISSN - 1439-4227
DOI - 10.1002/cbic.201490001
Subject(s) - substrate (aquarium) , cover (algebra) , chemistry , crystallography , stereochemistry , biology , ecology , engineering , mechanical engineering
The inside cover picture shows the substrate entrances of StDAPDH, which are shown on p. 217 ff. by D. Zhu and co‐workers to contribute to its unique substrate profile. Tunnel 1 is the entrance for the larger substrate, meso ‐DAP, which exists in all enzymes of the DAPDH family. Tunnel 2, with Met152 at its bottleneck, is found in the crystal structures of StDAPDH; through this, smaller pyruvate/ D ‐alanine can bind and enter the catalytic cavity.