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3.1.4.37: 2',3'-cyclic-nucleotide 3'-phosphodiesterase

This is an abbreviated version!
For detailed information about 2',3'-cyclic-nucleotide 3'-phosphodiesterase, go to the full flat file.

Word Map on EC 3.1.4.37

Reaction

nucleoside 2',3'-cyclic phosphate
+
H2O
=
Nucleoside 2'-phosphate

Synonyms

2',3'-cyclic AMP phosphodiesterase, 2',3'-cyclic nucleoside monophosphate phosphodiesterase, 2',3'-cyclic nucleotide 3'-phosphodiesterase, 2',3'-cyclic nucleotide 3'-phosphohydrolase, 2',3'-cyclic nucleotide phosphodiesterase, 2',3'-cyclic nucleotide phosphohydrolase, 2',3'-cyclic nucleotide-3'-phosphodiesterase, 2',3'-cyclic nucleotide-3'-phosphohydrolase, 2',3'-cyclic phosphodiesterase, 2',3'-cyclic-nucleotide 3'-phosphodiesterase type I, 2':3'-CNMP-3'-ase, 2':3'-cyclic nucleotide 3'-phosphodiesterase, 3DMA, CNP, CNP1, CNP2, CNPase, CNPase I, cyclic 2',3'-nucleotide 3'-phosphodiesterase, cyclic 2',3'-nucleotide phosphodiesterase, cyclic-CMP phosphodiesterase, DGC2, nucleoside-2':3'-cyclic-phosphate 2'-nucleotidohydrolase, PaAcpH, phosphodiesterase, cyclic 2',3'-nucleotide 3'-, PNKP, RocR, YtqI, YybT

ECTree

     3 Hydrolases
         3.1 Acting on ester bonds
             3.1.4 Phosphoric-diester hydrolases
                3.1.4.37 2',3'-cyclic-nucleotide 3'-phosphodiesterase

Crystallization

Crystallization on EC 3.1.4.37 - 2',3'-cyclic-nucleotide 3'-phosphodiesterase

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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
catalytic fragment of enzyme
-
catalytic domain, sittging drop vapor diffusion method, using 20-35% (w/v) PEG3350, PEG4000, or PEG6000 as precipitants and 50 mM Na acetate or 100 mM Na citrate, pH 3.0-5.0
phosphodiesterase domain of the enzyme with bound citrate, sulfate, NADP+, and 2-AMP, mixing of protein in 10 mM sodium citrate pH 5.5, 50 mM NaCl, 10% glycerol, and 1 mM DTT, with crystallization solution, X-ray diffraction structure determination and analysis at 1.74-2.4 A resolution, molecular replacement and modeling. Crystallization is only successful with sulfate or citrate present
structure analysis
-
wild-type and mutant enzymes complexed with substrate 2',3'-cyclic AMP, product 2'-AMP, and phosphorothioate analogues, and H230S mutant complexed with the substrate 2',3'-cNADP+, X-ray diffraction structure determination and analysis at 1.9-2.3 A resolution
modeling of enzyme N-terminal region and simulation of docking of nucleotides
-
structure analysis
-