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Information on EC 6.3.2.1 - pantoate-beta-alanine ligase (AMP-forming) and Organism(s) Escherichia coli and UniProt Accession P31663
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6.3.2.1 pantoate-beta-alanine ligase (AMP-forming)Specify your search results
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6-keto-pgf1
The taxonomic range for the selected organisms is: Escherichia coli
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Synonyms
synthetase, pantothenate, pantothenate synthetase, mtbps, pantoate-beta-alanine ligase, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
D-Pantoate:beta-alanine ligase (AMP-forming)
-
-
-
-
Pantoate activating enzyme
-
-
-
-
pantoate-beta-alanine ligase
-
-
-
-
Pantoic-activating enzyme
-
-
-
-
Pantothenate synthetase
Synthetase, pantothenate
-
-
-
-
Pantothenate synthetase
-
-
-
-
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
ATP + (R)-pantoate + beta-alanine = AMP + diphosphate + (R)-pantothenate
bi uni uni bi ping pong mechanism
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
carboxylic acid amide formation
-
-
-
-
carboxamide formation
-
-
-
-
PATHWAY SOURCE
PATHWAYS
BRENDA
KEGG
-
-
SYSTEMATIC NAME
IUBMB Comments
(R)-pantoate:beta-alanine ligase (AMP-forming)
-
CAS REGISTRY NUMBER
COMMENTARY
9023-49-8
-
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
ATP + (R)-pantoate + beta-alanine
AMP + diphosphate + (R)-pantothenate
-
-
-
?
ATP + (R)-pantoate + beta-alanine
?
-
formation of pantothenic acid, an important member of the B vitamins
-
-
?
CTP + (R)-pantoate + beta-alanine
CMP + diphosphate + (R)-pantothenate
-
14% of the activity relative to ATP
-
-
?
GTP + (R)-pantoate + beta-alanine
GMP + diphosphate + (R)-pantothenate
-
12% of the activity relative to ATP
-
-
?
ITP + (R)-pantoate + beta-alanine
IMP + diphosphate + (R)-pantothenate
-
14% of the activity relative to ATP
-
-
?
UTP + (R)-pantoate + beta-alanine
UMP + diphosphate + (R)-pantothenate
-
16% of the activity relative to ATP
-
-
?
ATP + (R)-pantoate + beta-alanine
AMP + diphosphate + (R)-pantothenate
-
-
-
?
ATP + (R)-pantoate + beta-alanine
AMP + diphosphate + (R)-pantothenate
-
-
-
?
ATP + (R)-pantoate + beta-alanine
AMP + diphosphate + (R)-pantothenate
-
-
-
-
?
ATP + (R)-pantoate + beta-alanine
AMP + diphosphate + (R)-pantothenate
-
-
-
?
ATP + (R)-pantoate + beta-alanine
AMP + diphosphate + (R)-pantothenate
-
-
-
-
?
ATP + (R)-pantoate + beta-alanine
AMP + diphosphate + (R)-pantothenate
-
synthesis of pantothenate, the essential precursor to coenzyme A
-
-
?
ATP + (R)-pantoate + beta-alanine
AMP + diphosphate + (R)-pantothenate
-
Bi Uni Uni Bi kinetic mechanism. Enzyme displays non-allosteric behavior
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
ATP + (R)-pantoate + beta-alanine
?
-
formation of pantothenic acid, an important member of the B vitamins
-
-
?
ATP + (R)-pantoate + beta-alanine
AMP + diphosphate + (R)-pantothenate
-
-
-
?
ATP + (R)-pantoate + beta-alanine
AMP + diphosphate + (R)-pantothenate
-
-
-
-
?
ATP + (R)-pantoate + beta-alanine
AMP + diphosphate + (R)-pantothenate
-
synthesis of pantothenate, the essential precursor to coenzyme A
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
K+
Mg2+
Mn2+
NH4+
Mg2+
-
divalent cation required, Mg2+ or Mn2+, Km: 2.0 mM. Optimal concentration: 10 mM, inhibition above
Mn2+
-
divalent cation required, Mg2+ or Mn2+. Optimal concentration: 5 mM, inhibition above
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
(2RS)-5'-O-(3,3-dimethyl-2-hydroxy-4-methoxybutyrylsulfamoyl)adenosine
-
3,3-dimethyl-2-oxobutyric acid 5-(6-aminopurin-9-yl)-3,4-dihydroxytetrahydrofuran-2-ylmethyl ester
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0008
(2RS)-5'-O-(2-hydroxy-4-methoxybutyrylsulfamoyl) adenosine
25°C
1.9
3,3-dimethyl-2-oxobutyric acid 5-(6-aminopurin-9-yl)-3,4-dihydroxytetrahydrofuran-2-ylmethyl ester
25°C
0.065
(2RS)-5'-O-(3,3-dimethyl-2-aminobutyrylsulfamoyl)adenosine
25°C
0.03
(2RS)-5'-O-(3,3-dimethyl-2-hydroxy-4-methoxybutyrylsulfamoyl)adenosine
25°C
0.054
(2RS)-5'-O-(3,3-dimethyl-2-hydroxy-4-methoxybutyrylsulfamoyl)adenosine
25°C
0.144
(2RS)-5'-O-(3,3-dimethyl-2-hydroxy-4-methoxybutyrylsulfamoyl)adenosine
25°C
0.0003
(2RS)-5'-O-(3,3-dimethyl-2-hydroxybutyrylsulfamoyl)adenosine
25°C
0.0008
(2RS)-5'-O-(3,3-dimethyl-2-hydroxybutyrylsulfamoyl)adenosine
25°C
0.0011
(2RS)-5'-O-(3,3-dimethyl-2-hydroxybutyrylsulfamoyl)adenosine
25°C
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
20 - 50
-
20°C: about 60% of maximal activity, 50°C, about 25% of maximal activity
30 - 45
-
30°C: maximal activity, 37°C: 90% of maximal activity, 45°C: 60% of maximal activity
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
dimer
-
molecular dynamics simulations show that the functional dynamics of the enzyme are dominated by motions of a flexible gate loop in the N-terminal domain and of the C-terminal domain. The gate loop motions dominate in Mycobacterium tuberculosis pantothenate synthetase while the C-terminal domain motion dominates in Escherichia coli pantothenate synthetase. Simulations also show that the correlated motions of the domains are severely compromised in the monomeric forms
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
tertiary structure of the dimeric N-terminal domain of Escherichia coli pantothenate synthetase, to a resolution of 1.7 A, shows a second molecule of pantoate bound in the ATP-binding pocket. Pantoate binding to the ATP-binding site induces large changes in structure, mainly for backbone and side chain atoms of residues in the ATP binding HXGH(34-37) motif. ATP stoichiometrically displaces pantoate from the ATP-binding site
crystal structures of pantothenate synthetase complexed with diphosphomethylphosphonic acid adenosyl ester and pantoate resolved at 1.6 A and of apo Escherichia coli pantothenate synthetase resolved at 1.70 A are used as the initial structures for the simulations
-
native and selenomethionine labeled PS, hanging drop vapor diffusion, hanging drops are composed of equal volumes of PS and reservoir solutions consisting of 50 mM Tris-HCl, pH 8.0, 4%-6% polyethylene glycol 4000, crystals appeare at 19°C after 2-4 days, crystals diffract to 1.7 A
-
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
D63G
-
mutation increases the mobility of the gate loop in Escherichia coli pantothenate synthetase
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
gene panC, recombinant expression as His-tagged enzyme, and expression in and complementation of the Arabidopsis thaliana knockout mutant phenotype by heterologous expression of Escherichia coli PTS, the panC transgene increases the total PTS activity in leaves of trangenic plants by up to 500fold but does not affect the steady-state level of pantothenate, overview
-
overexpression as a fusion protein with cytochrome b5 in Escherichia coli BL21(DE3). The advantages of the cytochrome b5 fusion system are its high expression levels in both rich and minimal medium, high solubility, stability, ease of purification, small size, and characteristic color
-
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Cronan, J.E.; Littel, K.J.; Jackowski, S.
Genetic and biochemical analyses of pantothenate biosynthesis in Escherichia coli and Salmonella typhimurium
J. Bacteriol.
149
916-922
1982
Escherichia coli, Salmonella enterica subsp. enterica serovar Typhimurium
Cronan, J.E.
Enzymatic synthesis of beta-[U-14C]alanine and D-[1,2,3-14C]pantothenate of high specific radioactivity
Anal. Biochem.
103
377-380
1980
Escherichia coli
Miyatake, K.; Nakano, Y.; Kitaoka, S.
Pantothenate synthetase from Escherichia coli [D-pantoate:beta-alanine ligase (AMP-forming), EC 6.3.2.1]
Methods Enzymol.
62
215-219
1979
Escherichia coli
Miyatake, K.; Nakano, Y.; Kitaoka, S.
Enzymological properties of pantothenate synthetase from Escherichia coli B
J. Nutr. Sci. Vitaminol.
24
243-253
1978
Escherichia coli
Miyatake, K.; Nakano, Y.; Kitaoka, S.
Some properties of pantothenate synthetase partially purified from Escherichia coli B
Bull. Univ. Osaka Prefect
27
57-67
1975
Escherichia coli
-
Miyatake, K.; Nakano, Y.; Kitaoka, S.
Pantothenate synthetase of Escherichia coli B. I. Physicochemical properties
J. Biochem.
79
673-678
1976
Escherichia coli, Escherichia coli B / ATCC 11303
Miyatake, K.; Nakano, Y.; Kitaoka, S.
Isotopic determination and optimum reaction conditions of pantothenic acid synthetase
Agric. Biol. Chem.
37
1205-1207
1973
Escherichia coli
-
Baillie, A.C.; Cornell, C.L.; Wright, B.J.; Wright, K.
Synthesis of potential inhibitors of the enzyme pantothenate synthetase
Tetrahedron Lett.
33
5133-5136
1992
Escherichia coli
-
von Delft, F.; Lewendon, A.; Dhanaraj, V.; Blundell, T.L.; Abell, C.; Smith, A.G.
The crystal structure of E. coli pantothenate synthetase confirms it as a member of the cytidylyltransferase superfamily
Structure
9
439-450
2001
Escherichia coli
Mitra, A.; Chakrabarti, K.S.; Hameed, M.S.S.; Srinivas, K.V.; Kumar, G.S.; Sarma, S.P.
High level expression of peptides and proteins using cytochrome b5 as a fusion host
Protein Expr. Purif.
41
84-97
2005
Escherichia coli
Jonczyk, R.; Genschel, U.
Molecular adaptation and allostery in plant pantothenate synthetases
J. Biol. Chem.
281
37435-37446
2006
Arabidopsis thaliana, Escherichia coli
Tuck, K.L.; Saldanha, S.A.; Birch, L.M.; Smith, A.G.; Abell, C.
The design and synthesis of inhibitors of pantothenate synthetase
Org. Biomol. Chem.
4
3598-3610
2006
Escherichia coli (P31663)
Jonczyk, R.; Ronconi, S.; Rychlik, M.; Genschel, U.
Pantothenate synthetase is essential but not limiting for pantothenate biosynthesis in Arabidopsis
Plant Mol. Biol.
66
1-14
2008
Escherichia coli, Arabidopsis thaliana (Q9FKB3), Arabidopsis thaliana
Chakrabarti, K.S.; Thakur, K.G.; Gopal, B.; Sarma, S.P.
X-ray crystallographic and NMR studies of pantothenate synthetase provide insights into the mechanism of homotropic inhibition by pantoate
FEBS J.
277
697-712
2010
Escherichia coli (P31663), Escherichia coli
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