Abstract:
:Mevalonate (MVA) metabolism provides the isoprenoids used in archaeal lipid biosynthesis. In synthesis of isopentenyl diphosphate, the classical MVA pathway involves decarboxylation of mevalonate diphosphate, while an alternate pathway has been proposed to involve decarboxylation of mevalonate monophosphate. To identify the enzymes responsible for metabolism of mevalonate 5-phosphate to isopentenyl diphosphate in Haloferax volcanii, two open reading frames (HVO_2762 and HVO_1412) were selected for expression and characterization. Characterization of these proteins indicated that one enzyme is an isopentenyl phosphate kinase that forms isopentenyl diphosphate (in a reaction analogous to that of Methanococcus jannaschii MJ0044). The second enzyme exhibits a decarboxylase activity that has never been directly attributed to this protein or any homologous protein. It catalyzes the synthesis of isopentenyl phosphate from mevalonate monophosphate, a reaction that has been proposed but never demonstrated by direct experimental proof, which is provided in this account. This enzyme, phosphomevalonate decarboxylase (PMD), exhibits strong inhibition by 6-fluoromevalonate monophosphate but negligible inhibition by 6-fluoromevalonate diphosphate (a potent inhibitor of the classical mevalonate pathway), reinforcing its selectivity for monophosphorylated ligands. Inhibition by the fluorinated analog also suggests that the PMD utilizes a reaction mechanism similar to that demonstrated for the classical MVA pathway decarboxylase. These observations represent the first experimental demonstration in H. volcanii of both the phosphomevalonate decarboxylase and isopentenyl phosphate kinase reactions that are required for an alternate mevalonate pathway in an archaeon. These results also represent, to our knowledge, the first identification and characterization of any phosphomevalonate decarboxylase.
journal_name
J Bacterioljournal_title
Journal of bacteriologyauthors
Vannice JC,Skaff DA,Keightley A,Addo JK,Wyckoff GJ,Miziorko HMdoi
10.1128/JB.01230-13subject
Has Abstractpub_date
2014-03-01 00:00:00pages
1055-63issue
5eissn
0021-9193issn
1098-5530pii
JB.01230-13journal_volume
196pub_type
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journal_title:Journal of bacteriology
pub_type: 杂志文章
doi:10.1128/JB.143.3.1384-1394.1980
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journal_title:Journal of bacteriology
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doi:10.1128/jb.169.7.3251-3259.1987
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journal_title:Journal of bacteriology
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doi:10.1128/JB.100.3.1208-1217.1969
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pub_type: 杂志文章
doi:10.1128/jb.172.2.678-685.1990
更新日期:1990-02-01 00:00:00
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journal_title:Journal of bacteriology
pub_type: 杂志文章
doi:10.1128/JB.131.3.821-829.1977
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journal_title:Journal of bacteriology
pub_type: 杂志文章
doi:10.1128/JB.181.20.6238-6246.1999
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pub_type: 杂志文章
doi:10.1128/jb.173.2.801-809.1991
更新日期:1991-01-01 00:00:00
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pub_type: 杂志文章
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更新日期:2001-03-01 00:00:00
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pub_type: 杂志文章
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更新日期:1983-10-01 00:00:00
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更新日期:1995-07-01 00:00:00
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pub_type: 杂志文章
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journal_title:Journal of bacteriology
pub_type: 杂志文章
doi:10.1128/JB.86.3.355-362.1963
更新日期:1963-09-01 00:00:00
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pub_type: 杂志文章
doi:10.1128/JB.159.1.57-62.1984
更新日期:1984-07-01 00:00:00