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Literature summary extracted from

  • Pandey, B.; Grover, S.; Goyal, S.; Kumari, A.; Singh, A.; Jamal, S.; Kaur, J.; Grover, A.
    Alanine mutation of the catalytic sites of pantothenate synthetase causes distinct conformational changes in the ATP binding region (2018), Sci. Rep., 8, 903 .
    View publication on PubMedView publication on EuropePMC

Protein Variants

EC Number Protein Variants Comment Organism
6.3.2.1 H44A site-directed mutagenesis, the mutant shows reduced catalytic activity compared to the wild-type enzyme Mycobacterium tuberculosis
6.3.2.1 H47A site-directed mutagenesis, the mutant shows only weak interactions between ATP and enzyme leading to reduced protein catalytic activity compared to wild-type Mycobacterium tuberculosis
6.3.2.1 K160A site-directed mutagenesis, the mutant shows only weak interactions between ATP and enzyme leading to reduced protein catalytic activity compared to wild-type Mycobacterium tuberculosis
6.3.2.1 additional information ATP is strongly bound to the catalytic core of the wild-type enzyme, limiting its movement to form a stable complex as compared to enzyme mutants Mycobacterium tuberculosis
6.3.2.1 N69A site-directed mutagenesis, mutant shows reduced catalytic activity compared to the wild-type enzyme Mycobacterium tuberculosis
6.3.2.1 Q164A site-directed mutagenesis, mutant shows reduced catalytic activity compared to the wild-type enzyme Mycobacterium tuberculosis
6.3.2.1 Q72A site-directed mutagenesis, mutant shows reduced catalytic activity compared to the wild-type enzyme Mycobacterium tuberculosis

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
6.3.2.1 Mg2+ required Mycobacterium tuberculosis

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
6.3.2.1 ATP + (R)-pantoate + beta-alanine Mycobacterium tuberculosis
-
 AMP + diphosphate + (R)-pantothenate
-
 ?
6.3.2.1 ATP + (R)-pantoate + beta-alanine Mycobacterium tuberculosis ATCC 25618 / H37Rv
-
 AMP + diphosphate + (R)-pantothenate
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
6.3.2.1 Mycobacterium tuberculosis P9WIL5
-
-
6.3.2.1 Mycobacterium tuberculosis ATCC 25618 / H37Rv P9WIL5
-
-

Reaction

EC Number Reaction Comment Organism Reaction ID
6.3.2.1 ATP + (R)-pantoate + beta-alanine = AMP + diphosphate + (R)-pantothenate the enzyme catalyzes the ATP-dependent condensation of pantoate with beta-alanine via a pantoyl adenylate intermediate and follows a bi uni uni bi ping pong kinetic mechanism. The Mg2+ dependent reaction involves two sequential steps. Initially binding of ATP with pantoate, leads to formation of pantoyl adenylate and release of diphosphate. Second step involves nucleophilic attack by beta-alanine on the active carbonyl group of pantoyl adenylate and subsequent release of AMP and pantothenate Mycobacterium tuberculosis
a

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
6.3.2.1 ATP + (R)-pantoate + beta-alanine
-
 Mycobacterium tuberculosis AMP + diphosphate + (R)-pantothenate
-
 ?
6.3.2.1 ATP + (R)-pantoate + beta-alanine
-
 Mycobacterium tuberculosis ATCC 25618 / H37Rv AMP + diphosphate + (R)-pantothenate
-
 ?

Synonyms

EC Number Synonyms Comment Organism
6.3.2.1 PanC
-
 Mycobacterium tuberculosis
6.3.2.1 Pantothenate synthetase
-
 Mycobacterium tuberculosis

Cofactor

EC Number Cofactor Comment Organism Structure
6.3.2.1 ATP ATP is strongly bound to the catalytic core of the wild-type enzyme, limiting its movement to form a stable complex, ATP-enzyme binding structure analysis, molecular mechanism, detailed overview. Molecular dynamics simulations and free energy calculations Mycobacterium tuberculosis

General Information

EC Number General Information Comment Organism
6.3.2.1 malfunction alanine mutation of the catalytic sites of pantothenate synthetase causes distinct conformational changes in the ATP binding region. Analysis of the molecular mechanism of decreased affinity of the enzyme for ATP caused by alanine mutations using molecular dynamics simulations and free energy calculations Mycobacterium tuberculosis
6.3.2.1 additional information significance and importance of conserved active site residues including His44, His47, Asn69, Gln72, Lys160 and Gln164 in substrate binding and formation of pantoyl adenylate intermediate. Molecular dynamics simulations of enzyme PS-ATP complex, substrate binding pocket and residue interactions analysis Mycobacterium tuberculosis