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2.7.7.3: pantetheine-phosphate adenylyltransferase

This is an abbreviated version!
For detailed information about pantetheine-phosphate adenylyltransferase, go to the full flat file.

Word Map on EC 2.7.7.3

Reaction

ATP
+
pantetheine 4'-phosphate
=
diphosphate
+
3'-dephospho-CoA

Synonyms

3'-dephospho-CoA pyrophosphorylase, 4'-phosphopantetheine adenylyltransferase, 4-phosphopantetheine adenylyltransferase, CoaD, dephospho-CoA pyrophosphorylase, dephospho-coenzyme A pyrophosphorylase, Enterococcus faecalis PPAT, More, pantetheine phosphate adenylyltransferase, phosphopantetheine adenylyltransferase, PPAT

ECTree

     2 Transferases
         2.7 Transferring phosphorus-containing groups
             2.7.7 Nucleotidyltransferases
                2.7.7.3 pantetheine-phosphate adenylyltransferase

Disease

Disease on EC 2.7.7.3 - pantetheine-phosphate adenylyltransferase

Please use the Disease Search for a specific query.
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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Cross Infection
Umbrella Sampling and X-ray Crystallographic Analysis Unveil an Arg-Asp Gate Facilitating Inhibitor Binding Inside Phosphopantetheine Adenylyltransferase Allosteric Cleft.
Pulmonary Disease, Chronic Obstructive
Rapid countermeasure discovery against Francisella tularensis based on a metabolic network reconstruction.
Respiratory Insufficiency
Umbrella Sampling and X-ray Crystallographic Analysis Unveil an Arg-Asp Gate Facilitating Inhibitor Binding Inside Phosphopantetheine Adenylyltransferase Allosteric Cleft.
Tuberculosis
Design of Novel Phosphopantetheine Adenylyltransferase Inhibitors: a Potential New Approach to Tackle Mycobacterium tuberculosis.
Kinetic, Thermodynamic, and Structural Insight into the Mechanism of Phosphopantetheine Adenylyltransferase from Mycobacterium tuberculosis.
Rhombohedral crystals of Mycobacterium tuberculosis phosphopantetheine adenylyltransferase.
Structure of Mycobacterium tuberculosis phosphopantetheine adenylyltransferase in complex with the feedback inhibitor CoA reveals only one active-site conformation.
Substrate-induced asymmetry and channel closure revealed by the apoenzyme structure of Mycobacterium tuberculosis phosphopantetheine adenylyltransferase.
X-ray study of the conformational changes in the molecule of phosphopantetheine adenylyltransferase from Mycobacterium tuberculosis during the catalyzed reaction.