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Information on EC 4.1.1.99 - phosphomevalonate decarboxylase and Organism(s) Haloferax volcanii and UniProt Accession D4GXZ3

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EC Tree
     4 Lyases
         4.1 Carbon-carbon lyases
             4.1.1 Carboxy-lyases
                4.1.1.99 phosphomevalonate decarboxylase
IUBMB Comments
The enzyme participates in a mevalonate pathway that occurs in halophilic archaea. The activity is also present in eubacteria of the Chloroflexi phylum. cf. EC 4.1.1.33, diphosphomevalonate decarboxylase, and EC 4.1.1.110, bisphosphomevalonate decarboxylase.
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This record set is specific for:
Haloferax volcanii
UNIPROT: D4GXZ3
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Word Map
The taxonomic range for the selected organisms is: Haloferax volcanii
The expected taxonomic range for this enzyme is: Halobacteria
Synonyms
phosphomevalonate decarboxylase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SYSTEMATIC NAME
IUBMB Comments
ATP:(R)-5-phosphomevalonate carboxy-lyase (adding ATP; isopentenyl-phosphate-forming)
The enzyme participates in a mevalonate pathway that occurs in halophilic archaea. The activity is also present in eubacteria of the Chloroflexi phylum. cf. EC 4.1.1.33, diphosphomevalonate decarboxylase, and EC 4.1.1.110, bisphosphomevalonate decarboxylase.
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
ATP + mevalonate 5-phosphate
ADP + phosphate + isopentenyl phosphate + CO2
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 + mevalonate 5-phosphate
ADP + phosphate + isopentenyl phosphate + CO2
show the reaction diagram
the enzyme is required for the alternate mevalonate pathway in an archaea
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
KCl
activity is not strongly dependent on KCl over a 0 to 4 M range
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
6-fluoromevalonate 5'-phosphate
negligible inhibition by 6-fluoromevalonate diphosphate (a potent inhibitor of the classical mevalonate pathway), reinforcing its selectivity for monophosphorylated ligands
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.289
ATP
pH 7.5, 30°C
0.075
mevalonate 5-phosphate
pH 7.5, 30°C
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.016
6-fluoromevalonate 5'-phosphate
Haloferax volcanii
pH 7.5, 30°C
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
37328
x * 37328, His-tagged enzyme, matrix-assisted laser desorption ionization-time of flight mass spectrometry
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
x * 37328, His-tagged enzyme, matrix-assisted laser desorption ionization-time of flight mass spectrometry
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
expression in Haloferax volcanii H1209
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
synthesis
isopentenol production in Escherichia coli by utilizing phosphomevalonate decarboxylase and Escherchia coli-endogenous phosphatase AphA. The enzymes bypass the isopentenyl diphosphate mevalonate pathways, have reduced energetic requirements, are further decoupled from intrinsic regulation, and are free from isopentenyl diphosphate-related toxicity. Reduced aeration rate has less impact on the bypass pathway than the original mevalonate pathway. The performance of the bypass pathway is primarily determined by the activity of phosphomevalonate decarboxylase
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Vannice, J.C.; Skaff, D.A.; Keightley, A.; Addo, J.K.; Wyckoff, G.J.; Miziorko, H.M.
Identification in Haloferax volcanii of phosphomevalonate decarboxylase and isopentenyl phosphate kinase as catalysts of the terminal enzyme reactions in an archaeal alternate mevalonate pathway
J. Bacteriol.
196
1055-1063
2014
Haloferax volcanii (D4GXZ3), Haloferax volcanii, Haloferax volcanii DSM 3757 (D4GXZ3)
Manually annotated by BRENDA team
Kang, A.; George, K.W.; Wang, G.; Baidoo, E.; Keasling, J.D.; Lee, T.S.
Isopentenyl diphosphate (IPP)-bypass mevalonate pathways for isopentenol production
Metab. Eng.
34
25-35
2016
Haloferax volcanii (D4GXZ3), Haloferax volcanii DSM 3757 (D4GXZ3)
Manually annotated by BRENDA team