Sandbox Reserved 1501: Difference between revisions
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This is a default text for your page ''''''. Click above on '''edit this page''' to modify. Be careful with the < and > signs. | This is a default text for your page ''''''. Click above on '''edit this page''' to modify. Be careful with the < and > signs. | ||
You may include any references to papers as in: the use of JSmol in Proteopedia <ref>DOI 10.1002/ijch.201300024</ref> or to the article describing Jmol <ref>PMID:21638687</ref> to the rescue. | You may include any references to papers as in: the use of JSmol in Proteopedia <ref>DOI 10.1002/ijch.201300024</ref> or to the article describing Jmol <ref>PMID:21638687</ref> to the rescue. | ||
Encoded in the ''Saccharomyces cerevisiae'' (strain ATCC 204508 / S288c) gene CYB2 the protein Flavocytochrome b(2) | |||
It is an Oxidoreductase categorized according to IUB as EC: 1.1.2.3. | |||
== Function == | == Function == | ||
Flavocytochrome b(2) (Arg289Lys mutant) from ''Saccharomyces cerevisiae'' is an oxidoreductase that couples dehydrogenation of L-lactate to cytochrome c reduction by electron transfer. It is one step of the bacterial lactate metabolic pathway. | |||
Similar oxidants that can be used to perform the reaction in vitro are ferricyanide, phenozine methosulfate and quinone [experiment first performed 1963 by Nygaard, later in 1966 described by Symons and Burgoyne]. | |||
The Yeasts L-Lactate Dehydrogenase can be inhibited by heavy metals, oxygen, glycerate, oxalate, malate, phenylpyruvate and fatty acids [Nygaard 1963]. | |||
The Enzyme shows a specificity for L-lactate but none for the D-isomer or -hydroxybutyrate. | |||
== Relevance == | == Relevance == | ||
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== Structural highlights == | == Structural highlights == | ||
Global Symmetry Cyclic - C4 | |||
Global Stoichiometry Homotetramer A4 | |||
Flavocytochrome b(2) is a tetrameric enzyme [Jacq and Lederer, 1972]. Each of the four identical subunits is composed by one single polypeptide chain. | |||
Each subunit contains a binding site for the selectively non-covalently binding of the cofactor FM3- (FlavinMonoNucleotide), | |||
https://www.wikiwand.com/de/Flavinmononukleotid | |||
as well as one in with the iron complexed in the tetrapyrrole ring interacts with heme b(2-) cofactor [Risler and Groudinsky, 1973]. | |||
https://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:60344 | |||
The amino acid sequence in the heme binding region was first determined by Guidard et al. (1974). | |||
For every subunit the crystallized preparation analysis determined a molecular weight of the chain of 36 kD [Appleby and Morton] and the chain of 21 kD [Jacq and Lederer, 1974]. | |||
Arginin 289 to Lysine | |||
http://www.worthington-biochem.com/yldhs/ | |||
