“Threonine synthase”的意思、由来-开放百科全书

词条

Threonine synthase

释义

Structural studies
References

{{enzyme
| Name = threonine synthase
| EC_number = 4.2.3.1
| CAS_number = 9023-97-6
| IUBMB_EC_number = 4/2/3/1
| GO_code = 0004795
| image =
| width =
| caption =
}}

In enzymology, a threonine synthase ({{EC number|4.2.3.1}}) is an enzyme that catalyzes the chemical reaction

O-phospho-L-homoserine + H₂O L-threonine + phosphate

Thus, the two substrates of this enzyme are O-phospho-L-homoserine and H₂O, whereas its two products are L-threonine and phosphate.

This enzyme belongs to the family of lyases, specifically those carbon-oxygen lyases acting on phosphates. The systematic name of this enzyme class is O-phospho-L-homoserine phosphate-lyase (adding water L-threonine-forming). Other names in common use include threonine synthetase, and O-phospho-L-homoserine phospho-lyase (adding water). This enzyme participates in glycine, serine and threonine metabolism and vitamin B₆ metabolism. It employs one cofactor, pyridoxal phosphate.

Structural studies

As of late 2007, 7 structures have been solved for this class of enzymes, with PDB accession codes {{PDB link|1UIM}}, {{PDB link|1UIN}}, {{PDB link|1V7C}}, {{PDB link|1VB3}}, {{PDB link|2C2B}}, {{PDB link|2C2G}}, and {{PDB link|2D1F}}.

References

{{cite journal |vauthors=FLAVIN M, SLAUGHTER C | date = 1960 | title = Purification and properties of threonine synthetase of Neurospora | journal = J. Biol. Chem. | volume = 235 | pages = 1103–8 | pmid = 13823379 }}

3 : EC 4.2.3|Pyridoxal phosphate enzymes|Enzymes of known structure

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