“Protein-glutamine gamma-glutamyltransferase”的意思、由来-开放百科全书

词条

Protein-glutamine gamma-glutamyltransferase

释义

Nomenclature
Structural studies
References

{{enzyme
| Name = protein-glutamine gamma-glutamyltransferase
| EC_number = 2.3.2.13
| CAS_number = 80146-85-6
| IUBMB_EC_number = 2/3/2/13
| GO_code = 0003810
| image =
| width =
| caption =
}}{{Orphan|date=February 2009}}

In enzymology, a protein-glutamine gamma-glutamyltransferase ({{EC number|2.3.2.13}}) is an enzyme that catalyzes the chemical reaction

protein glutamine + alkylamine protein N₅-alkylglutamine + NH₃

Thus, the two substrates of this enzyme are protein glutamine and alkylamine, whereas its two products are protein N(5)-alkylglutamine and NH₃.

This enzyme participates in complement and coagulation cascades and Huntington's disease. It employs one cofactor, calcium.

Nomenclature

This enzyme belongs to the family of transferases, specifically the aminoacyltransferases. The systematic name of this enzyme class is protein-glutamine:amine gamma-glutamyltransferase. Other names in common use include:

factor XIIIa,
fibrin stabilizing factor,
fibrinoligase,
glutaminylpeptide gamma-glutamyltransferase,
polyamine transglutaminase,
R-glutaminyl-peptide:amine gamma-glutamyl transferase
tissue transglutaminase, and
transglutaminase.

Structural studies

As of late 2007, 19 structures have been solved for this class of enzymes, with PDB accession codes {{PDB link|1EVU}}, {{PDB link|1EX0}}, {{PDB link|1F13}}, {{PDB link|1FIE}}, {{PDB link|1G0D}}, {{PDB link|1GGT}}, {{PDB link|1GGU}}, {{PDB link|1GGY}}, {{PDB link|1IU4}}, {{PDB link|1KV3}}, {{PDB link|1L9M}}, {{PDB link|1L9N}}, {{PDB link|1NUD}}, {{PDB link|1NUF}}, {{PDB link|1NUG}}, {{PDB link|1QRK}}, {{PDB link|1RLE}}, {{PDB link|1SGX}}, and {{PDB link|1VJJ}}.

References

{{refbegin}}* {{cite journal | vauthors = Folk JE, Chung SI | year = 1973 | title = Molecular and catalytic properties of transglutaminases | journal = Adv. Enzymol. Relat. Areas Mol. Biol. | volume = 38 | pages = 109–91 | pmid = 4151471 | doi = 10.1002/9780470122839.ch3 | series = Advances in Enzymology - and Related Areas of Molecular Biology | isbn = 978-0-470-12283-9 }}

{{cite journal | vauthors = Folk JE, Cole PW | year = 1966 | title = Mechanism of action of guinea pig liver transglutaminase. I Purification and properties of the enzyme: identification of a functional cysteine essential for activity | journal = J. Biol. Chem. | volume = 241 | pages = 5518–25 | pmid = 5928192 | issue = 23 }}
{{cite journal | vauthors = Folk JE, Finlayson JS | year = 1977 | title = The epsilon-(gamma-glutamyl)lysine crosslink and the catalytic role of transglutaminases | journal = Adv. Protein. Chem. | volume = 31 | pages = 1–133 | pmid = 73346 | doi = 10.1016/S0065-3233(08)60217-X | series = Advances in Protein Chemistry | isbn = 978-0-12-034231-0 }}
{{cite journal | vauthors = Takahashi N, Takahashi Y, Putnam FW | year = 1986 | title = Primary structure of blood coagulation factor XIIIa (fibrinoligase, transglutaminase) from human placenta | journal = Proc. Natl. Acad. Sci. U.S.A. | volume = 83 | pages = 8019–23 | pmid = 2877456 | doi = 10.1073/pnas.83.21.8019 | issue = 21 | pmc = 386858 }}

3 : EC 2.3.2|Calcium enzymes|Enzymes of known structure

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