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Information on EC 4.1.1.99 - phosphomevalonate decarboxylase for references in articles please use BRENDA:EC4.1.1.99
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EC Tree
IUBMB Comments The enzyme participates in a mevalonate pathway that occurs in archaea other than the extreme acidophiles of the Thermoplasmatales order. cf. EC 4.1.1.110, bisphosphomevalonate decarboxylase.
The expected taxonomic range for this enzyme is: Halobacteria
Synonyms
HVO_1412 , MvaD, PMD,
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ATP + (R)-5-phosphomevalonate = ADP + phosphate + isopentenyl phosphate + CO2
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ATP:(R)-5-phosphomevalonate carboxy-lyase (adding ATP; isopentenyl-phosphate-forming)
The enzyme participates in a mevalonate pathway that occurs in archaea other than the extreme acidophiles of the Thermoplasmatales order. cf. EC 4.1.1.110, bisphosphomevalonate decarboxylase.
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ATP + mevalonate 5-phosphate
ADP + phosphate + isopentenyl phosphate + CO2
ATP + mevalonate 5-phosphate
ADP + phosphate + isopentenyl phosphate + CO2
the enzyme is required for the alternate mevalonate pathway in an archaea
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?
ATP + mevalonate 5-phosphate
ADP + phosphate + isopentenyl phosphate + CO2
very weak activity with mevalonate and even less with mevalonate 5-diphosphate
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?
ATP + mevalonate 5-phosphate
ADP + phosphate + isopentenyl phosphate + CO2
the enzyme is required for the alternate mevalonate pathway in an archaea
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-
?
ATP + mevalonate 5-phosphate
ADP + phosphate + isopentenyl phosphate + CO2
very weak activity with mevalonate and even less with mevalonate 5-diphosphate
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?
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ATP + mevalonate 5-phosphate
ADP + phosphate + isopentenyl phosphate + CO2
ATP + mevalonate 5-phosphate
ADP + phosphate + isopentenyl phosphate + CO2
the enzyme is required for the alternate mevalonate pathway in an archaea
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-
?
ATP + mevalonate 5-phosphate
ADP + phosphate + isopentenyl phosphate + CO2
the enzyme is required for the alternate mevalonate pathway in an archaea
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?
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KCl
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activity is not strongly dependent on KCl over a 0 to 4 M range
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6-fluoromevalonate 5'-phosphate
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negligible inhibition by 6-fluoromevalonate diphosphate (a potent inhibitor of the classical mevalonate pathway), reinforcing its selectivity for monophosphorylated ligands
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0.075
mevalonate 5-phosphate
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pH 7.5, 30°C
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0.016
6-fluoromevalonate 5'-phosphate
Haloferax volcanii
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pH 7.5, 30°C
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UniProt
brenda
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UniProt
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PMD_HALVD
Haloferax volcanii (strain ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM B-1768 / DS2)
324
0
35417
Swiss-Prot
A0A4D6GRN2_HALS9
Halobacterium salinarum (strain ATCC 33171 / DSM 3754 / JCM 8978 / NBRC 102687 / NCIMB 764 / 91-R6)
325
0
34749
TrEMBL
A0A510N509_HALSA
Halobacterium salinarum (strain ATCC 700922 / JCM 11081 / NRC-1)
325
0
34749
TrEMBL
Q3ISK5_NATPD
Natronomonas pharaonis (strain ATCC 35678 / DSM 2160 / CIP 103997 / NBRC 14720 / NCIMB 2260 / Gabara)
324
0
35472
TrEMBL
G0LGL3_HALWC
Haloquadratum walsbyi (strain DSM 16854 / JCM 12705 / C23)
324
0
35143
TrEMBL
M1XPZ3_NATM8
Natronomonas moolapensis (strain DSM 18674 / JCM 14361 / 8.8.11)
323
0
35075
TrEMBL
A0A5Q0UNU4_9EURY
323
0
34924
TrEMBL
B0R3Q6_HALS3
Halobacterium salinarum (strain ATCC 29341 / DSM 671 / R1)
325
0
34749
TrEMBL
A0A343TH50_9EURY
331
0
36161
TrEMBL
Q18K00_HALWD
Haloquadratum walsbyi (strain DSM 16790 / HBSQ001)
324
0
35128
TrEMBL
A0A0U5H0P9_9EURY
326
0
35543
TrEMBL
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37328
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x * 37328, His-tagged enzyme, matrix-assisted laser desorption ionization-time of flight mass spectrometry
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?
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x * 37328, His-tagged enzyme, matrix-assisted laser desorption ionization-time of flight mass spectrometry
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x * 37328, His-tagged enzyme, matrix-assisted laser desorption ionization-time of flight mass spectrometry
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expression in Escherichia coli
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expression in Haloferax volcanii H1209
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synthesis
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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
synthesis
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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
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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)
brenda
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)
brenda
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Enzyme Nomenclature
4.1.1.99 phosphomevalonate decarboxylase
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