CoB—CoM heterodisulfide reductase

CoB—CoM heterodisulfide reductase
Identifiers
EC number	1.8.98.1
CAS number	116515-35-6
Databases
IntEnz	IntEnz view
BRENDA	BRENDA entry
ExPASy	NiceZyme view
KEGG	KEGG entry
MetaCyc	metabolic pathway
PRIAM	profile
PDB structures	RCSB PDB PDBe PDBsum
Gene Ontology	AmiGO / EGO
Search PMC articles PubMed articles

In enzymology, a CoB—CoM heterodisulfide reductase (EC 1.8.98.1) is an enzyme that catalyzes the chemical reaction

coenzyme B + coenzyme M + methanophenazine $\rightleftharpoons$ N-{7-[(2-sulfoethyl)dithio]heptanoyl}-O₃-phospho-L-threonine + dihydromethanophenazine

The 3 substrates of this enzyme are coenzyme B, coenzyme M, and methanophenazine, whereas its two products are [[N-{7-[(2-sulfoethyl)dithio]heptanoyl}-O₃-phospho-L-threonine]] and dihydromethanophenazine.

This enzyme belongs to the family of oxidoreductases, specifically those acting on a sulfur group of donors with other, known, acceptors. The systematic name of this enzyme class is coenzyme B:coenzyme M:methanophenazine oxidoreductase. Other names in common use include heterodisulfide reductase, and soluble heterodisulfide reductase. This enzyme participates in folate biosynthesis.

References

• Hedderich R, Berkessel A, Thauer RK (1990). "Purification and properties of heterodisulfide reductase from Methanobacterium thermoautotrophicum (strain Marburg)". Eur. J. Biochem. 193 (1): 255–61. doi:10.1111/j.1432-1033.1990.tb19331.x. PMID 2121478. 
• Abken HJ, Tietze M, Brodersen J, Baumer S, Beifuss U, Deppenmeier U (1998). "Isolation and characterization of methanophenazine and function of phenazines in membrane-bound electron transport of Methanosarcina mazei Go1". J. Bacteriol. 180 (8): 2027–32. PMC 107126. PMID 9555882. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=107126. 
• Simianu M, Murakami E, Brewer JM, Ragsdale SW (1998). "Purification and properties of the heme- and iron-sulfur-containing heterodisulfide reductase from Methanosarcina thermophila". Biochemistry. 37 (28): 10027–39. doi:10.1021/bi9726483. PMID 9665708. 
• Murakami E, Deppenmeier U, Ragsdale SW (2001). "Characterization of the intramolecular electron transfer pathway from 2-hydroxyphenazine to the heterodisulfide reductase from Methanosarcina thermophila". J. Biol. Chem. 276 (4): 2432–9. doi:10.1074/jbc.M004809200. PMID 11034998. 

This EC 1.8 enzyme-related article is a stub. You can help Wikipedia by expanding it.v · Categories: Oxidoreductase stubs EC 1.8.98 Enzymes of unknown structure Wikimedia Foundation. 2010. Игры ⚽ Поможем написать реферат Arthur–Merlin protocol CoBoosting Look at other dictionaries: CoB-CoM heterodisulfide reductase — In enzymology, a CoB CoM heterodisulfide reductase (EC number|1.8.98.1) is an enzyme that catalyzes the chemical reaction:coenzyme B + coenzyme M + methanophenazine ightleftharpoons N {7 [(2 sulfoethyl)dithio] heptanoyl} O3 phospho L threonine +… …   Wikipedia List of EC numbers (EC 1) — This list contains a list of EC numbers for the first group, EC 1, oxidoreducatases, placed in numerical order as determined by the Nomenclature Committee of the International Union of Biochemistry and Molecular Biology.EC 1.1 Acting on the CH OH …   Wikipedia Oxidoreductase — In biochemistry, an oxidoreductase is an enzyme that catalyzes the transfer of electrons from one molecule (the reductant, also called the hydrogen or electron donor) to another (the oxidant, also called the hydrogen or electron acceptor). This… …   Wikipedia Dihydrolipoamide dehydrogenase — PDB rendering based on 1zy8 …   Wikipedia Coenzyme-B sulfoethylthiotransferase — Identifiers EC number 2.8.4.1 Databases IntEnz IntEnz view …   Wikipedia Coenzyme M — is a coenzyme required for methyl transfer reactions in the metabolism of methanogens.[1][2] The coenzyme is an anion with the formula …   Wikipedia 18+ © Academic, 2000-2024 Contact us: Technical Support, Advertising Dictionaries export, created on PHP, Joomla, Drupal, WordPress, MODx. Mark and share Search through all dictionaries Translate… Search Internet Share the article and excerpts Direct link … Do a right-click on the link above and select “Copy Link”