“Lipoyl synthase”的意思、由来-开放百科全书

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Lipoyl synthase

释义

Nomenclature
References

{{enzyme
| Name = Lipoyl synthase
| EC_number = 2.8.1.8
| CAS_number = 189398-80-9
| IUBMB_EC_number = 2/8/1/8
| GO_code = 0016992
| image =
| width =
| caption =
}}

In enzymology, a lipoyl synthase ({{EC number|2.8.1.8}}) is an enzyme that catalyzes the chemical reaction

protein N₆-(octanoyl)lysine + 2 sulfur + 2 S-adenosyl-L-methionine protein N₆-(lipoyl)lysine + 2 L-methionine + 2 5'-deoxyadenosine

The 3 substrates of this enzyme are protein N6-(octanoyl)lysine, sulfur, and S-adenosyl-L-methionine, whereas its 3 products are protein N6-(lipoyl)lysine, L-methionine, and 5'-deoxyadenosine.

This enzyme belongs to the family of transferases, specifically the sulfurtransferases, which transfer sulfur-containing groups. This enzyme participates in lipoic acid metabolism, where it performs the final step in lipoic acid biosynthesis. It is an iron-sulfur protein containing two 4Fe-4S clusters. It is localized to the mitochondria in certain studied eukaryotic model organisms.

Nomenclature

The systematic name of this enzyme class is protein N6-(octanoyl)lysine:sulfur sulfurtransferase. Other names in common use include:

LS,
LipA,
lipoate synthase, and
protein 6-N-(octanoyl)lysine:sulfur sulfurtransferase.

References

{{cite journal |vauthors=Cicchillo RM, Booker SJ | date = 2005 | title = Mechanistic investigations of lipoic acid biosynthesis in Escherichia coli: both sulfur atoms in lipoic acid are contributed by the same lipoyl synthase polypeptide | journal = J. Am. Chem. Soc. | volume = 127 | pages = 2860–1 | pmid = 15740115 | doi = 10.1021/ja042428u | issue = 9 }}
{{cite journal |vauthors=Vanden Boom TJ, Reed KE, Cronan JE | date = 1991 | title = Lipoic acid metabolism in Escherichia coli: isolation of null mutants defective in lipoic acid biosynthesis, molecular cloning and characterization of the E. coli lip locus, and identification of the lipoylated protein of the glycine cleavage system | journal = J. Bacteriol. | volume = 173 | pages = 6411–20 | pmid = 1655709 | issue = 20 | pmc = 208974 }}
{{cite journal |vauthors=Zhao X, Miller JR, Jiang Y, Marletta MA, Cronan JE | date = 2003 | title = Assembly of the covalent linkage between lipoic acid and its cognate enzymes | journal = Chem. Biol. | volume = 10 | pages = 1293–302 | pmid = 14700636 | doi = 10.1016/j.chembiol.2003.11.016 | issue = 12 }}
{{cite journal |vauthors=Souder MG, Tu L, Booker SJ | date = 2004 | title = Lipoyl synthase requires two equivalents of S-adenosyl-L-methionine to synthesize one equivalent of lipoic acid | journal = Biochemistry | volume = 43 | pages = 6378–86 | pmid = 15157071 | doi = 10.1021/bi049528x | issue = 21 }}
{{cite journal |vauthors=Jordan SW, Cronan JE | date = 1997 | title = A new metabolic link. The acyl carrier protein of lipid synthesis donates lipoic acid to the pyruvate dehydrogenase complex in Escherichia coli and mitochondria | journal = J. Biol. Chem. | volume = 272 | pages = 17903–6 | pmid = 9218413 | doi = 10.1074/jbc.272.29.17903 | issue = 29 }}
{{cite journal |vauthors=Broderick JB, Cronan JE, Marletta MA | date = 2000 | title = Escherichia coli LipA is a lipoyl synthase: in vitro biosynthesis of lipoylated pyruvate dehydrogenase complex from octanoyl-acyl carrier protein | journal = Biochemistry | volume = 39 | pages = 15166–78 | pmid = 11106496 | doi = 10.1021/bi002060n | issue = 49 }}
{{cite journal | author = Perham RN | date = 2000 | title = Swinging arms and swinging domains in multifunctional enzymes: catalytic machines for multistep reactions | journal = Annu. Rev. Biochem. | volume = 69 | issue = 1 | pages = 961–1004 | pmid = 10966480 | doi = 10.1146/annurev.biochem.69.1.961 }}

{{refend}}{{Sulfur-containing group transferases}}{{Enzymes}}{{Portal bar|Molecular and Cellular Biology|border=no}}{{2.8-enzyme-stub}}

2 : EC 2.8.1|Enzymes of unknown structure

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