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Information on EC 6.3.2.1 - pantoate-beta-alanine ligase (AMP-forming) and Organism(s) Staphylococcus aureus and UniProt Accession Q2FV22

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Staphylococcus aureus
UNIPROT: Q2FV22 not found.
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The taxonomic range for the selected organisms is: Staphylococcus aureus
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Synonyms
synthetase, pantothenate, pantothenate synthetase, mtbps, pantoate-beta-alanine ligase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Pantothenate synthetase
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D-Pantoate:beta-alanine ligase (AMP-forming)
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-
-
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Pantoate activating enzyme
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-
-
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pantoate-beta-alanine ligase
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-
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Pantoic-activating enzyme
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-
-
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Pantothenate synthetase
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-
-
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Synthetase, pantothenate
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-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
carboxylic acid amide formation
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-
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carboxamide formation
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-
-
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SYSTEMATIC NAME
IUBMB Comments
(R)-pantoate:beta-alanine ligase (AMP-forming)
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CAS REGISTRY NUMBER
COMMENTARY hide
9023-49-8
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SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
ATP + (R)-pantoate + beta-alanine
AMP + diphosphate + (R)-pantothenate
show the reaction diagram
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-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1.5
(R)-pantoate
co-substrate: beta-alanine, pH 8.0, 30°C
1.5
beta-Alanine
co-substrate: (R)-pantoate, pH 8.0, 30°C
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
structures of the apoenzyme and the reaction intermediate complex are determined by X-ray crystallography to resolutions of 2.5 A and 1.85 A, respectively. Structural analysis indicate that the apoenzyme adopts an open and relatively mobile structure, while the complex structure is closed and entirely rigid. In the complex structure, pantothenate synthetase and acetate are bound in the active site. Acetate might mimic the substrate beta-alanine. Therefore, the complex structure might represent a catalytic state poised for in-line nucleophilic attack on pantothenate synthetase
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
using Ni-NTA chromatography
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli as a His-tagged fusion protein
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Satoh, A.; Konishi, S.; Tamura, H.; Stickland, H.G.; Whitney, H.M.; Smith, A.G.; Matsumura, H.; Inoue, T.
Substrate-induced closing of the active site revealed by the crystal structure of pantothenate synthetase from Staphylococcus aureus
Biochemistry
49
6400-6410
2010
Staphylococcus aureus (Q2FV22), Staphylococcus aureus
Manually annotated by BRENDA team