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
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2.7.7.3
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ppats
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penultimate
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dpcoa
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pantothen
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pyrophosphate
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hexameric
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3\'-dephospho-coa
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nucleotidyltransferase
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dephosphocoenzyme
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phosphopantothenoylcysteine
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medicine
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drug development
- 2.7.7.3
-
ppats
-
penultimate
-
dpcoa
-
pantothen
- pyrophosphate
-
hexameric
-
3\'-dephospho-coa
-
nucleotidyltransferase
-
dephosphocoenzyme
-
phosphopantothenoylcysteine
- medicine
- drug development
Reaction
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
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Disease
Disease on EC 2.7.7.3 - pantetheine-phosphate adenylyltransferase
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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.
Tuberculosis
Kinetic, Thermodynamic, and Structural Insight into the Mechanism of Phosphopantetheine Adenylyltransferase from Mycobacterium tuberculosis.
Tuberculosis
Rhombohedral crystals of Mycobacterium tuberculosis phosphopantetheine adenylyltransferase.
Tuberculosis
Structure of Mycobacterium tuberculosis phosphopantetheine adenylyltransferase in complex with the feedback inhibitor CoA reveals only one active-site conformation.
Tuberculosis
Substrate-induced asymmetry and channel closure revealed by the apoenzyme structure of Mycobacterium tuberculosis phosphopantetheine adenylyltransferase.
Tuberculosis
X-ray study of the conformational changes in the molecule of phosphopantetheine adenylyltransferase from Mycobacterium tuberculosis during the catalyzed reaction.
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