Dihydroneopterin triphosphate epimerase of Escherichia coli: purification, genetic cloning, and expression.
The enzyme catalyzing the epimerization at position 2' of dihydroneopterin triphosphate was purified by a factor of about 10,000 from cell extract of Escherichia coli. The cognate gene was cloned, sequenced, expressed, and mapped to kb 2427 on the E. coli chromosome.
Haussmann
C
C
Institut für Organische Chemie und Biochemie, Technische Universität München, Garching, Federal Republic of Germany.
Rohdich
F
F
Lottspeich
F
F
Eberhardt
S
S
Scheuring
J
J
Mackamul
S
S
Bacher
A
A
D000595:Amino Acid Sequence; D001426:Bacterial Proteins / Q000235:genetics*; D001483:Base Sequence; D003001:Cloning, Molecular; D004926:Escherichia coli / Q000201:enzymology / Q000235:genetics*; D029968:Escherichia coli Proteins; D005798:Genes, Bacterial; D008969:Molecular Sequence Data; D019798:Neopterin / Q000031:analogs & derivatives; D011621:Pteridines / Q000378:metabolism*; D019998:Racemases and Epimerases / Q000235:genetics* / Q000302:isolation & purification; D015183:Restriction Mapping; D017422:Sequence Analysis, DNA; D017386:Sequence Homology, Amino Acid
D001426:Bacterial Proteins; D029968:Escherichia coli Proteins; D011621:Pteridines; C013490:dihydroneopterin triphosphate; D019798:Neopterin; D019998:Racemases and Epimerases; C023128:folX protein, E coli