Tetrahydromethanopterin

Structural formula
General
Surname	Tetrahydromethanopterin
other names	H 4 MPT
Molecular formula	C 30 H 45 N 6 O 16 P
External identifiers / databases
PubChem	5459995
ChemSpider	4573696
Wikidata	Q704048
properties
Molar mass	776.68 g · mol -1
safety instructions
GHS hazard labeling ; no classification available
GHS hazard labeling ; no classification available
	As far as possible and customary, SI units are used. Unless otherwise noted, the data given apply to standard conditions .

Tetrahydromethanopterin ( THMPT , H ₄ MPT ) is a coenzyme in methanogenesis . It was discovered in various microorganisms, where it plays an important role in the metabolism of methyl groups . A modified form of THMPT is tetrahydrosarcinapterin (with the glutamyl residue bound to 2-hydroxyglutaric acid ) and the more well-known tetrahydrofolic acid is related to THMPT.

properties

Tetrahydromethanopterin containing the methyl group, which is reduced in the course of methanogenesis and then coenzyme M is transmitted.

Compared to tetrahydrofolate, methyl-THMPT is more difficult to reduce due to the lack of a carbonyl group on the phenyl ring . The reduction is mediated by an iron-sulfur cluster free hydrogenase .

In the C1 metabolism , N -formyl methanofuran gives the C1 group to the N5 of the pteridine, creating formyl-THMPT. The formyl group condenses to the cationic methenyl-THMPT, which is then reduced to the methylene-THMPT. Methylene-THMPT is reduced to methyl-THMPT by the methylene-THMPT reductase using coenzyme F420 . Methyl-THMPT transfers the methyl group to coenzyme M by methyl-THMPT: coenzyme-M-methyltransferase.

Web links

The one-carbon carrier tetrahydromethanopterin in enzymes

Individual evidence

↑ This substance has either not yet been classified with regard to its hazardousness or a reliable and citable source has not yet been found.
^ ^A ^b Thauer RK: Biochemistry of methanogenesis: a tribute to Marjory Stephenson . 1998 Marjory Stephenson Prize Lecture . In: Microbiology . 144, No. Pt 9, September 1998, pp. 2377-406. doi : 10.1099 / 00221287-144-9-2377 . PMID 9782487 .
↑ ^a ^b Korbas M, Vogt S, Meyer-Klaucke W, et al. : The iron-sulfur cluster-free hydrogenase (Hmd) is a metalloenzyme with a novel iron binding motif . In: J. Biol. Chem. . 281, No. 41, October 2006, pp. 30804-13. doi : 10.1074 / jbc.M605306200 . PMID 16887798 .
↑ Acharya P, Warkentin E, Ermler U, Thauer RK, Shima S: The structure of formylmethanofuran: tetrahydromethanopterin formyltransferase in complex with its coenzymes . In: J. Mol. Biol. . 357, No. 3, March 2006, pp. 870-9. doi : 10.1016 / j.jmb.2006.01.015 . PMID 16466742 .

[NV-1] This substance has either not yet been classified with regard to its hazardousness or a reliable and citable source has not yet been found.

[Thauer-2] A ^b Thauer RK: Biochemistry of methanogenesis: a tribute to Marjory Stephenson . 1998 Marjory Stephenson Prize Lecture . In: Microbiology . 144, No. Pt 9, September 1998, pp. 2377-406. doi : 10.1099 / 00221287-144-9-2377 . PMID 9782487 .

[Korbas-3] Korbas M, Vogt S, Meyer-Klaucke W, et al. : The iron-sulfur cluster-free hydrogenase (Hmd) is a metalloenzyme with a novel iron binding motif . In: J. Biol. Chem. . 281, No. 41, October 2006, pp. 30804-13. doi : 10.1074 / jbc.M605306200 . PMID 16887798 .

[4] Acharya P, Warkentin E, Ermler U, Thauer RK, Shima S: The structure of formylmethanofuran: tetrahydromethanopterin formyltransferase in complex with its coenzymes . In: J. Mol. Biol. . 357, No. 3, March 2006, pp. 870-9. doi : 10.1016 / j.jmb.2006.01.015 . PMID 16466742 .