An HD domain phosphohydrolase active site tailored for oxetanocin-A biosynthesis
HD domain phosphohydrolase enzymes are characterized by a conserved set of histidine and aspartate residues that coordinate an active site metallocenter. Despite the important roles these enzymes play in nucleotide metabolism and signal transduction, few have been both biochemically and structurally...
Huvudupphovsmän: | Zhong, Aoshu, Liu, Hung-wen, Rabb, Jennifer, Drennan, Catherine L., Kang, Gyung Hoon |
---|---|
Övriga upphovsmän: | Massachusetts Institute of Technology. Department of Biology |
Materialtyp: | Artikel |
Språk: | en_US |
Publicerad: |
National Academy of Sciences (U.S.)
2017
|
Länkar: | http://hdl.handle.net/1721.1/109092 https://orcid.org/0000-0002-7437-6217 https://orcid.org/0000-0001-5486-2755 https://orcid.org/0000-0003-2117-3528 |
Liknande verk
Liknande verk
-
A B12-dependent radical SAM enzyme involved in oxetanocin A biosynthesis
av: Zhong, Aoshu, et al.
Publicerad: (2018) -
SYNTHESIS OF OXETANOCIN
av: Wilson, F, et al.
Publicerad: (1990) -
Vitamin B 12 in the spotlight again
av: Bridwell-Rabb, Jennifer, et al.
Publicerad: (2020) -
Multiple substrate recognition by yeast diadenosine and diphosphoinositol polyphosphate phosphohydrolase through phosphate clamping
av: Márquez-Moñino, MÁ, et al.
Publicerad: (2021) -
Cobalamin-Dependent Radical S -Adenosylmethionine Enzymes: Capitalizing on Old Motifs for New Functions
av: Bridwell-Rabb, Jennifer, et al.
Publicerad: (2022)