A lag-phase in the reduction of flavin dependent thymidylate synthase (FDTS) revealed a mechanistic missing link.
An unexpected substrate-dependent lag-phase, found in the single turnover reduction of FDTS bound flavin, sheds light on the molecular mechanism of this alternative thymidylate synthase.
Mason
Aaron
A
Department of Chemistry, University of Iowa, Iowa City, IA, USA. amnon-kohen@uiowa.edu
Agrawal
Nitish
N
Washington
M Todd
MT
Lesley
Scott A
SA
Kohen
Amnon
A
D001426:Bacterial Proteins / Q000378:metabolism; D003856:Deoxyuracil Nucleotides / Q000737:chemistry / Q000378:metabolism; D005182:Flavin-Adenine Dinucleotide / Q000378:metabolism*; D009249:NADP / Q000737:chemistry / Q000378:metabolism; D020124:Thermotoga maritima / Q000201:enzymology*; D013940:Thymidylate Synthase / Q000737:chemistry / Q000378:metabolism*
D001426:Bacterial Proteins; D003856:Deoxyuracil Nucleotides; D005182:Flavin-Adenine Dinucleotide; D009249:NADP; C007267:2'-deoxyuridylic acid; D013940:Thymidylate Synthase