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4-hydroxy-3-methylbut-2-en-1-yl diphosphate synthase

From Wikipedia, the free encyclopedia
(Redirected from HMB-PP synthase)
4-hydroxy-3-methylbut-2-en-1-yl diphosphate synthase
Identifiers
EC no.1.17.7.1
Databases
BRENDAenzyme data
ExPASyNiceZyme view
KEGGenzyme entry
MetaCycmetabolic pathway
Rheareactions
PDB structuresRCSB PDB PDBe PDBsum
Gene OntologyAmiGO / QuickGO
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PMCarticles
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NCBIproteins

4-hydroxy-3-methylbut-2-en-1-yl diphosphate synthase (HMB-PP synthase, IspG, EC 1.17.7.1) is an enzyme that catalyzes a redox reaction

+ 2 oxidised ferredoxin
 
 
 
H2O
Rightward reaction arrow with minor product(s) to top right
 
 
 
+ 2 reduced ferredoxin
 

The substrate of this enzyme is 2-C-methyl-D-erythritol 2,4-cyclodiphosphate (MEcPP) and the product is (E)-4-hydroxy-3-methylbut-2-en-1-yl diphosphate (HMB-PP). Electrons are donated by two reduced ferredoxin proteins per reaction.[1] The enzyme characterised from Thermosynechococcus elongatus contains an iron-sulfur cluster.[2][3][4]

The reaction is part of the non-mevalonate pathway (MEP pathway) of isoprenoid precursor biosynthesis.[5]

Nomenclature

[edit]

This enzyme is an oxidoreductase, specifically one acting on CH or CH2 groups with a disulfide as acceptor. The systematic name of this enzyme class is (E)-4-hydroxy-3-methylbut-2-en-1-yl-diphosphate:protein-disulfide oxidoreductase (hydrating).[6]

References

[edit]
  1. ↑ Hecht, Stefan; Eisenreich, Wolfgang; Adam, Petra; Amslinger, Sabine; Kis, Klaus; Bacher, Adelbert; Arigoni, Duilio; Rohdich, Felix (2001). "Studies on the nonmevalonate pathway to terpenes: The role of the GcpE (IspG) protein". Proceedings of the National Academy of Sciences. 98 (26): 14837–14842. doi:10.1073/pnas.201399298. PMC 64945. PMID 11752431.
  2. ↑ Okada, Ken; Hase, Toshiharu (2005). "Cyanobacterial Non-mevalonate Pathway". Journal of Biological Chemistry. 280 (21): 20672–20679. doi:10.1074/jbc.M500865200. PMID 15792953.
  3. ↑ Seemann, Myriam; Wegner, Patrick; Schunemann, Volker; Bui, Bernadette Tse Sum; Wolff, Murielle; Marquet, Andrée; Trautwein, Alfred X.; Rohmer, Michel (2005). "Isoprenoid biosynthesis in chloroplasts via the methylerythritol phosphate pathway: The (E)-4-hydroxy-3-methylbut-2-enyl diphosphate synthase (GcpE) from Arabidopsis thaliana is a [4Fe?4S] protein". Journal of Biological Inorganic Chemistry. 10 (2): 131–137. doi:10.1007/s00775-004-0619-z. PMID 15650872.
  4. ↑ Seemann, Myriam; Bui, Bernadette Tse Sum; Wolff, Murielle; Tritsch, Denis; Campos, Narciso; Boronat, Albert; Marquet, Andrée; Rohmer, Michel (2002). "Isoprenoid Biosynthesis through the Methylerythritol Phosphate Pathway: The (E)-4-Hydroxy-3-methylbut-2-enyl Diphosphate Synthase (GcpE) is a [4Fe–4S] Protein". Angewandte Chemie International Edition. 41 (22): 4337–4339. doi:10.1002/1521-3773(20021115)41:22<4337::AID-ANIE4337>3.0.CO;2-K. PMID 12434382.
  5. ↑ Seemann, Myriam; Tse Sum Bui, Bernadette; Wolff, Murielle; Miginiac-Maslow, Myroslawa; Rohmer, Michel (2006). "Isoprenoid biosynthesis in plant chloroplasts via the MEP pathway: Direct thylakoid/Ferredoxin-dependent photoreduction of GcpE/IspG". FEBS Letters. 580 (6): 1547–1552. doi:10.1016/j.febslet.2006.01.082. PMID 16480720.
  6. ↑ Enzyme 1.17.7.1 at KEGG Pathway Database.