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Information on EC 6.3.2.26 - N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase and Organism(s) Thermococcus kodakarensis and UniProt Accession Q5JIZ8

for references in articles please use BRENDA:EC6.3.2.26
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EC Tree
IUBMB Comments
Requires Mg2+. The enzyme contains 4'-phosphopantetheine, which may be involved in the mechanism of the reaction. Forms part of the penicillin biosynthesis pathway (for pathway, click here).
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This record set is specific for:
Thermococcus kodakarensis
UNIPROT: Q5JIZ8
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Word Map
The taxonomic range for the selected organisms is: Thermococcus kodakarensis
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
Synonyms
acv synthetase, delta-(l-alpha-aminoadipyl)-l-cysteinyl-d-valine synthetase, phosphopantothenate synthetase, tk1686, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
phosphopantothenate synthetase
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ACV synthetase
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-
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DELTA-(alpha-aminoadipyl)cysteinylvaline synthetase
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delta-(L-alpha-aminoadipoyl)-L-cysteinyl-D-valine synthetase
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delta-L-(alpha-aminoadipyl)-L-cysteinyl-D-valine synthetase
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-
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L-(alpha-aminoadipyl)-L-cysteinyl-D-valine synthetase
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L-delta-(alpha-aminoadipoyl)-L-cysteinyl-D-valine synthetase
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synthetase, delta-(alpha-aminoadipyl)cysteinylvaline
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-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
carboxylic acid amid formation
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-
-
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peptide bond formation
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-
-
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SYSTEMATIC NAME
IUBMB Comments
L-2-aminohexanedioate:L-cysteine:L-valine ligase (AMP-forming, valine-inverting)
Requires Mg2+. The enzyme contains 4'-phosphopantetheine, which may be involved in the mechanism of the reaction. Forms part of the penicillin biosynthesis pathway (for pathway, click here).
CAS REGISTRY NUMBER
COMMENTARY hide
57219-73-5
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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)-4-phosphopantoate + beta-alanine
AMP + diphosphate + (R)-4'-phosphopantothenate
show the reaction diagram
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
ATP + (R)-4-phosphopantoate + beta-alanine
AMP + diphosphate + (R)-4'-phosphopantothenate
show the reaction diagram
the enzyme is involved in coenzyme A biosynthesis in the archaea
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-
?
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
4-phosphopantoate
substrate inhibition
ATP
substrate inhibition
additional information
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1.16
(R)-4-phosphopantoate
pH 6.5, 85°C
2.44
ATP
pH 6.5, 85°C
0.34
beta-Alanine
pH 6.5, 85°C
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
14.7
ATP, pH 6.5, 85°C
15.6
(R)-4-phosphopantoate, pH 6.5, 85°C
6.38
beta-alanine, pH 6.5, 85°C
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
65 - 95
activity continues to increase with temperature elevation from 65°C up to 95°C
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
70
6 h, no decrease in activity
80
half-life: 13.6 h
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
overexpressed in Escherichoa coli
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Ishibashi, T.; Tomita, H.; Yokooji, Y.; Morikita, T.; Watanabe, B.; Hiratake, J.; Kishimoto, A.; Kita, A.; Miki, K.; Imanaka, T.; Atomi, H.
A detailed biochemical characterization of phosphopantothenate synthetase, a novel enzyme involved in coenzyme A biosynthesis in the Archaea
Extremophiles
16
819-828
2012
Thermococcus kodakarensis (Q5JIZ8), Thermococcus kodakarensis
Manually annotated by BRENDA team