| 词条 | YgbB N terminal protein domain |
| 释义 |
| Symbol = YgbB | Name = YgbB | image = PDB 1vh8 EBI.jpg | width = | caption = crystal structure of a 2c-methyl-d-erythritol 2,4-cyclodiphosphate synthase | Pfam = PF02542 | Pfam_clan = | InterPro = IPR003526 | SMART = | PROSITE = | MEROPS = | SCOP = 1iv1 | TCDB = | OPM family = | OPM protein = | CAZy = | CDD = cd0554 }} In molecular biology, YgbB is a protein domain. This entry makes reference to a number of proteins from eukaryotes and prokaryotes which share this common N-terminal signature and appear to be involved in terpenoid biosynthesis. The YgbB protein is a putative enzyme thought to aid terpenoid and isoprenoid biosynthesis, a vital chemical in all living organisms. This protein domain is part of an enzyme which catalyses a reaction in a complex pathway.[1] FunctionThe YgbB protein domain has a main function of being involved in terpenoid and isoprenoid biosynthesis. BiochemistryMECDP (2-C-methyl-D-erythritol 2,4-cyclodiphosphate) synthetase, an enzyme in the non-mevalonate pathway of isoprenoid synthesis, isoprenoids being essential in all organisms. Isoprenoids can also be synthesized through the mevalonate pathway. The non-mevolante route is used by many bacteria and human pathogens, including Mycobacterium tuberculosis and Plasmodium falciparum. This route appears to involve seven enzymes. MECDP synthetase catalyses the intramolecular attack by a phosphate group on a diphosphate, with cytidine monophosphate (CMP) acting as the leaving group to give the cyclic diphosphate product MEDCP. The enzyme is a trimer with three active sites shared between adjacent copies of the protein. The enzyme also has two metal binding sites, the metals playing key roles in catalysis.[2] 1. ^{{cite journal |vauthors=Herz S, Wungsintaweekul J, Schuhr CA, Hecht S, Luttgen H, Sagner S, Fellermeier M, Eisenreich W, Zenk MH, Bacher A, Rohdich F | title = Biosynthesis of terpenoids: YgbB protein converts 4-diphosphocytidyl-2C-methyl-D-erythritol 2-phosphate to 2C-methyl-D-erythritol 2,4-cyclodiphosphate | journal = Proc. Natl. Acad. Sci. U.S.A. | volume = 97 | issue = 6 | pages = 2486–90 |date=March 2000 | pmid = 10694574 | pmc = 15955 | doi = 10.1073/pnas.040554697 | url = }} 2. ^{{cite journal |vauthors=Kishida H, Wada T, Unzai S, Kuzuyama T, Takagi M, Terada T, Shirouzu M, Yokoyama S, Tame JR, Park SY | title = Structure and catalytic mechanism of 2-C-methyl-D-erythritol 2,4-cyclodiphosphate (MECDP) synthase, an enzyme in the non-mevalonate pathway of isoprenoid synthesis | journal = Acta Crystallogr. D | volume = 59 | issue = Pt 1 | pages = 23–31 |date=January 2003 | pmid = 12499535 | doi = 10.1107/s0907444902017705| url = }} 1 : Protein domains |
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