Polyphosphatase activity of CthTTM, a bacterial triphosphate tunnel metalloenzyme. - Wikidata - wikimedia - TriplyDB

Polyphosphatase activity of CthTTM, a bacterial triphosphate tunnel metalloenzyme.

Polyphosphatase activity of CthTTM, a bacterial triphosphate tunnel metalloenzyme.

http://www.wikidata.org/entity/Q30157516

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mRNA capping: biological functions and applications Structure of bacterial LigD 3'-phosphoesterase unveils a DNA repair superfamily A Specific Inorganic Triphosphatase from Nitrosomonas europaea: STRUCTURE AND CATALYTIC MECHANISM Crystal Structure of Vaccinia Virus mRNA Capping Enzyme Provides Insights into the Mechanism and Evolution of the Capping Apparatus Thiamine triphosphatase and the CYTH superfamily of proteins.Crystal structure and biochemical analyses reveal that the Arabidopsis triphosphate tunnel metalloenzyme AtTTM3 is a tripolyphosphatase involved in root development.Structural Determinants for Substrate Binding and Catalysis in Triphosphate Tunnel Metalloenzymes.Nanomolar Inhibitors of Trypanosoma brucei RNA Triphosphatase.Enzyme Tunnels and Gates As Relevant Targets in Drug Design.High inorganic triphosphatase activities in bacteria and mammalian cells: identification of the enzymes involved.Nucleotide analogs and molecular modeling studies reveal key interactions involved in substrate recognition by the yeast RNA triphosphatase

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P2860

Polyphosphatase activity of CthTTM, a bacterial triphosphate tunnel metalloenzyme.

http://www.wikidata.org/entity/Q30157516

description

2008 nî lūn-bûn

@nan

2008 թուականի Սեպտեմբերին հրատարակուած գիտական յօդուած

@hyw

2008 թվականի սեպտեմբերին հրատարակված գիտական հոդված

@hy

2008年の論文

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2008年論文

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2008年論文

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2008年論文

@zh-hk

2008年論文

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2008年論文

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2008年论文

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name

Polyphosphatase activity of CthTTM, a bacterial triphosphate tunnel metalloenzyme.

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Polyphosphatase activity of CthTTM, a bacterial triphosphate tunnel metalloenzyme.

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type

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Polyphosphatase activity of CthTTM, a bacterial triphosphate tunnel metalloenzyme.

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Polyphosphatase activity of CthTTM, a bacterial triphosphate tunnel metalloenzyme.

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Polyphosphatase activity of CthTTM, a bacterial triphosphate tunnel metalloenzyme.

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Polyphosphatase activity of CthTTM, a bacterial triphosphate tunnel metalloenzyme.

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Journal of Biological Chemistry

P1476

Polyphosphatase activity of CthTTM, a bacterial triphosphate tunnel metalloenzyme.

@en

P2093

Ruchi Jain

http://www.w3.org/2001/XMLSchema#string

Stewart Shuman

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P2860

Molecular characterization of a specific thiamine triphosphatase widely expressed in mammalian tissues

The LEF-4 subunit of baculovirus RNA polymerase has RNA 5'-triphosphatase and ATPase activities.

Structural basis for the catalytic mechanism of mammalian 25-kDa thiamine triphosphatase

The catalytic domains of thiamine triphosphatase and CyaB-like adenylyl cyclase define a novel superfamily of domains that bind organic phosphates.

Structure and mechanism of yeast RNA triphosphatase: an essential component of the mRNA capping apparatus

The crystal structure of the cytosolic exopolyphosphatase from Saccharomyces cerevisiae reveals the basis for substrate specificity

Characterization of a trifunctional mimivirus mRNA capping enzyme and crystal structure of the RNA triphosphatase domain

A soluble exopolyphosphatase of Saccharomyces cerevisiae. Purification and characterization.

The long and short of it - polyphosphate, PPK and bacterial survival

Polyphosphate kinase is involved in stress-induced mprAB-sigE-rel signalling in mycobacteria

P304

31047-31057

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scholarly article

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10.1074/JBC.M805392200

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45

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283

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2008-09-08T00:00:00Z

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18782773

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2576530

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