Boonstra B, French C E, Wainwright I, Bruce N C
Institute of Biotechnology, University of Cambridge, Cambridge CB2 1QT, United Kingdom.
J Bacteriol. 1999 Feb;181(3):1030-4. doi: 10.1128/JB.181.3.1030-1034.1999.
The udhA gene of Escherichia coli was cloned and expressed in E. coli and found to encode an enzyme with soluble pyridine nucleotide transhydrogenase activity. The N-terminal end of the enzyme contains the fingerprint motif of a dinucleotide binding domain, not present in published E. coli genome sequences due to a sequencing error. E. coli is hereby the first organism reported to possess both a soluble and a membrane-bound pyridine nucleotide transhydrogenase.
大肠杆菌的udhA基因被克隆并在大肠杆菌中表达，发现其编码一种具有可溶性吡啶核苷酸转氢酶活性的酶。该酶的N末端含有二核苷酸结合结构域的指纹基序，由于测序错误，已发表的大肠杆菌基因组序列中不存在该基序。因此，大肠杆菌是首个被报道同时拥有可溶性和膜结合吡啶核苷酸转氢酶的生物体。
