A phosphate-binding histidine of binuclear metallophosphodiesterase enzymes is a determinant of 2',3'-cyclic nucleotide phosphodiesterase activity
about
Molecular bases of catalysis and ADP-ribose preference of human Mn2+-dependent ADP-ribose/CDP-alcohol diphosphatase and conversion by mutagenesis to a preferential cyclic ADP-ribose phosphohydrolaseA Mycobacterial Cyclic AMP Phosphodiesterase That Moonlights as a Modifier of Cell Wall PermeabilityStructural and functional analysis of the Lmo2642 cyclic nucleotide phosphodiesterase from Listeria monocytogenesStructure and mechanism of the 2',3' phosphatase component of the bacterial Pnkp-Hen1 RNA repair systemThe YmdB Phosphodiesterase Is a Global Regulator of Late Adaptive Responses in Bacillus subtilisReversible acetylation and inactivation of Mycobacterium tuberculosis acetyl-CoA synthetase is dependent on cAMPMycobacterium tuberculosis Rv3586 (DacA) is a diadenylate cyclase that converts ATP or ADP into c-di-AMP.From complete genome sequence to 'complete' understanding?Deletion of the cyclic di-AMP phosphodiesterase gene (cnpB) in Mycobacterium tuberculosis leads to reduced virulence in a mouse model of infection.The non-catalytic "cap domain" of a mycobacterial metallophosphoesterase regulates its expression and localization in the cell.Characterization of Danio rerio Mn2+-dependent ADP-ribose/CDP-alcohol diphosphatase, the structural prototype of the ADPRibase-Mn-like protein family.Biochemical and functional characterization of SpdA, a 2', 3'cyclic nucleotide phosphodiesterase from Sinorhizobium meliloti.A Drosophila metallophosphoesterase mediates deglycosylation of rhodopsin.Structural and enzymatic characterization of the streptococcal ATP/diadenosine polyphosphate and phosphodiester hydrolase Spr1479/SapH.Cyclic AMP signalling in mycobacteria: redirecting the conversation with a common currencyStructure-activity relationships in human RNA 3'-phosphate cyclase.Metallophosphoesterases: structural fidelity with functional promiscuity.Revisiting bacterial cyclic nucleotide phosphodiesterases: cyclic AMP hydrolysis and beyond.Ca(II) Binding Regulates and Dominates the Reactivity of a Transition-Metal-Ion-Dependent Diesterase from Mycobacterium tuberculosis.Role of Phosphate Transport System Component PstB1 in Phosphate Internalization by Nostoc punctiforme.Mechanistic insights into the manganese-dependent phosphodiesterase activity of yeast Dbr1 with bis-p-nitrophenylphosphate and branched RNA substrates.CpdA is involved in amino acid metabolism in Shewanella oneidensis MR-1.Determination of the catalytic activity of binuclear metallohydrolases using isothermal titration calorimetry.Architecture of the U6 snRNP reveals specific recognition of 3'-end processed U6 snRNA.
P2860
Q27313411-EB6DDDF7-5F91-4FA4-B0D6-F96AC73D9E29Q27657658-B56A3480-095D-4A78-9424-DF7F890E035BQ27666542-FC45FBF0-3639-4D6A-9F1C-47E976405ABFQ27677432-90A56F8D-BC6D-47AA-AE4F-A41A7720C4C1Q27680466-61199C25-AFD2-4EA4-A816-87658E2CDF09Q28487076-B0489B02-FA9C-4C9F-BDB1-BBD7A2A51348Q31058151-5CFA8685-2067-4D09-A0A6-27C789164576Q33637109-3B9B1ACD-E7AE-4BA1-B91D-9296EF9C40A7Q33870379-7F25868A-43F5-4ACB-9896-0B74138D7EEDQ34070493-81E13465-15EF-4819-B168-64456DB73538Q34359672-C8972E8D-F0E7-47A6-A23D-F0EAA9775860Q35054345-C4BD374D-704D-44DB-A52D-053832A69810Q35214900-8392C00D-6829-4745-B2CC-6D269A368B37Q35372209-9DEA6678-C3C2-421B-9F70-2F664FE03921Q37202695-90F0230E-3D4B-4B65-961C-84455A10D4C7Q37344501-61BF8674-6328-4E3B-BF8C-34F932886131Q38402990-D1F2002D-43E7-4ED4-A54A-034E700690C7Q38596396-8B0DF5B1-456D-4DD2-8EDA-30CA2406CF17Q40216653-EC8F2842-7C64-4F6E-8E9D-0D2A528E1A7AQ41475337-106A42FF-9DC6-4598-AB13-B8FDF8A754A7Q45282935-C9BDA806-CB5B-48D7-9FE1-4E39996192B0Q47299078-FE0F8E30-746A-43EB-B5EB-303CD9BD04D7Q52764907-24799A29-DDC6-4B3C-8D75-52C25ABFD1A8Q55259305-7DC19515-075F-48F0-A7A3-B3E754E70EAC
P2860
A phosphate-binding histidine of binuclear metallophosphodiesterase enzymes is a determinant of 2',3'-cyclic nucleotide phosphodiesterase activity
description
2008 թուականի Նոյեմբերին հրատարակուած գիտական յօդուած
@hyw
2008 թվականի նոյեմբերին հրատարակված գիտական հոդված
@hy
article publié dans la revue scientifique Journal of Biological Chemistry
@fr
artículu científicu espublizáu en 2008
@ast
im November 2008 veröffentlichter wissenschaftlicher Artikel
@de
scientific journal article
@en
vedecký článok (publikovaný 2008/11/07)
@sk
vědecký článek publikovaný v roce 2008
@cs
wetenschappelijk artikel (gepubliceerd op 2008/11/07)
@nl
наукова стаття, опублікована в листопаді 2008
@uk
name
A phosphate-binding histidine ...... ide phosphodiesterase activity
@ast
A phosphate-binding histidine ...... ide phosphodiesterase activity
@en
A phosphate-binding histidine ...... ide phosphodiesterase activity
@nl
type
label
A phosphate-binding histidine ...... ide phosphodiesterase activity
@ast
A phosphate-binding histidine ...... ide phosphodiesterase activity
@en
A phosphate-binding histidine ...... ide phosphodiesterase activity
@nl
prefLabel
A phosphate-binding histidine ...... ide phosphodiesterase activity
@ast
A phosphate-binding histidine ...... ide phosphodiesterase activity
@en
A phosphate-binding histidine ...... ide phosphodiesterase activity
@nl
P2860
P356
P1476
A phosphate-binding histidine ...... ide phosphodiesterase activity
@en
P2093
Niroshika Keppetipola
P2860
P304
30942–30949
P356
10.1074/JBC.M805064200
P407
P577
2008-11-07T00:00:00Z