PMCC PMCC

Search tips
Search criteria

Advanced
Results 1-2 (2)
 

Clipboard (0)
None

Select a Filter Below

Journals
Authors
Year of Publication
Document Types
1.  2-(9H-Fluoren-9-yl)-4-(4-fluoro­anilino)-4-oxo­butanoic acid 
In the title compound, C23H18FNO3, the tricyclic 9-fluorenyl system is approximately planar (r.m.s. deviation = 0.0279 Å). The N—C(=O) bond length is comparatively short [1.359 (3) Å], which is typical for such conjugated systems. The N atom has a planar configuration [sum of bond angles= 359.8°] due to conjugation of its lone pair with the π-system of the carbonyl group. In the crystal, a three-dimensional network is formed through N—H⋯O and O—H⋯O hydrogen bonds between the amide and carb­oxy­lic acid groups and carbonyl O-atom acceptors.
doi:10.1107/S1600536813013779
PMCID: PMC3685102  PMID: 23795121
2.  Absence of Substrate Channeling between Active Sites in the Agrobacterium tumefaciens IspDF and IspE Enzymes of the Methyl Erythritol Phosphate Pathway† 
Biochemistry  2006;45(11):3548-3553.
The conversion of 2C-methyl-d-erythritol 4-phosphate (MEP) to 2C-methyl-d-erythritol 2,4-cyclodiphosphate (cMEDP) in the MEP entry into the isoprenoid biosynthetic pathway occurs in three consecutive steps catalyzed by the IspD, IspE, and IspF enzymes, respectively. In Agrobacterium tumefaciens the ispD and ispF genes are fused to encode a bifunctional enzyme that catalyzes the first (synthesis of 4-diphosphocytidyl-2-C-methyl d-erythritol) and third (synthesis of 2C-methyl-d-erythritol 2,4-cyclodiphosphate) steps. Sedimentation velocity experiments indicate that the bifunctional IspDF enzyme and the IspE protein associate in solution raising the possibility of substrate channeling among the active sites in these two proteins. Kinetic evidence for substrate channeling was sought by measuring the time courses for product formation during incubations of MEP, CTP, and ATP with the IspDF and IspE proteins with and without an excess of the inactive IspE (D152A) mutant in presence or absence of 30% (v/v) glycerol. The time dependencies indicate that the enzyme-generated intermediates are not transferred from the IspD active site in IspDF to the active site of IspE or from the active site in IspE to the active site in the IspF module of IspDF.
doi:10.1021/bi0520075
PMCID: PMC2516919  PMID: 16533036
bifunctional; IspDF; IspE; non-channeling

Results 1-2 (2)