“S-methyl-5'-thioadenosine phosphorylase”的意思、由来-开放百科全书

词条

S-methyl-5'-thioadenosine phosphorylase

释义

Structural studies
References

{{enzyme
| Name = S-methyl-5-thioadenosine phosphorylase
| EC_number = 2.4.2.28
| CAS_number = 61970-06-7
| IUBMB_EC_number = 2/4/2/28
| GO_code = 0017061
| image = 5tc8.jpg
| width = 270
| caption = S-methyl-5'-thioadenosine phosphorylase trimer, Human
}}

In enzymology, a S-methyl-5'-thioadenosine phosphorylase ({{EC number|2.4.2.28}}) is an enzyme that catalyzes the chemical reaction

S-methyl-5'-thioadenosine + phosphate adenine + S-methyl-5-thio-alpha-D-ribose 1-phosphate

Thus, the two substrates of this enzyme are S-methyl-5'-thioadenosine and phosphate, whereas its two products are adenine and S-methyl-5-thio-alpha-D-ribose 1-phosphate.

This enzyme belongs to the family of glycosyltransferases, specifically the pentosyltransferases. The systematic name of this enzyme class is S-methyl-5-thioadenosine:phosphate S-methyl-5-thio-alpha-D-ribosyl-transferase. Other names in common use include 5'-methylthioadenosine nucleosidase, 5'-deoxy-5'-methylthioadenosine phosphorylase, MTA phosphorylase, MeSAdo phosphorylase, MeSAdo/Ado phosphorylase, methylthioadenosine phosphorylase, methylthioadenosine nucleoside phosphorylase, 5'-methylthioadenosine:phosphate methylthio-D-ribosyl-transferase, and S-methyl-5-thioadenosine phosphorylase. This enzyme participates in methionine metabolism.

Structural studies

As of late 2007, 20 structures have been solved for this class of enzymes, with PDB accession codes {{PDB link|1CB0}}, {{PDB link|1CG6}}, {{PDB link|1JDS}}, {{PDB link|1JDT}}, {{PDB link|1JDU}}, {{PDB link|1JDV}}, {{PDB link|1JDZ}}, {{PDB link|1JE0}}, {{PDB link|1JE1}}, {{PDB link|1JP7}}, {{PDB link|1JPV}}, {{PDB link|1K27}}, {{PDB link|1ODI}}, {{PDB link|1ODJ}}, {{PDB link|1ODK}}, {{PDB link|1SD1}}, {{PDB link|1SD2}}, {{PDB link|1V4N}}, {{PDB link|1WTA}}, and {{PDB link|2A8Y}}.

References

{{cite journal | vauthors = Gambacorta A, Zappia V | date = 1979 | title = 5'-Methylthioadenosine phosphorylase from Caldariella acidophila Purification and properties | journal = Eur. J. Biochem. | volume = 101 | pages = 317–24 | pmid = 118001 | doi = 10.1111/j.1432-1033.1979.tb19723.x | issue = 2 }}
{{cite journal | author = Garbers DL | date = 1978 | title = Demonstration of 5'-methylthioadenosine phosphorylase activity in various rat tissues. Some properties of the enzyme from rat lung | journal = Biochim. Biophys. Acta | volume = 523 | pages = 82–93 | pmid = 415762 | issue = 1 | doi=10.1016/0005-2744(78)90011-6}}
{{cite journal | vauthors = Pegg AE, Williams-Ashman HG | date = 1969 | title = Phosphate-stimulated breakdown of 5'-methylthioadenosine by rat ventral prostate | journal = Biochem. J. | volume = 115 | pages = 241–7 | pmid = 5378381 | issue = 2 | pmc = 1185095 }}

2 : EC 2.4.2|Enzymes of known structure

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