“Peptidoglycan glycosyltransferase”的意思、由来-开放百科全书

词条

Peptidoglycan glycosyltransferase

释义

Structural studies
References

{{enzyme
| Name = peptidoglycan glycosyltransferase
| EC_number = 2.4.1.129
| CAS_number = 79079-04-2
| IUBMB_EC_number = 2/4/1/129
| GO_code = 0008955
| image =
| width =
| caption =
}}

In enzymology, a peptidoglycan glycosyltransferase ({{EC number|2.4.1.129}}) is an enzyme that catalyzes the chemical reaction

[GlcNAc-(1->4)-Mur₂Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)]n- diphosphoundecaprenol + GlcNAc-(1->4)-Mur₂Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)- diphosphoundecaprenol

⇌

[GlcNAc-(1->4)-Mur₂Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)]n⁺1- diphosphoundecaprenol + undecaprenyl diphosphate

The 4 substrates of this enzyme are

[GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)]n-,
diphosphoundecaprenol,
GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)-, and
diphosphoundecaprenol,

whereas its 3 products are

[GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)]n+1-,
diphosphoundecaprenol, and
undecaprenyl diphosphate.

This enzyme belongs to the family of glycosyltransferases, specifically the hexosyltransferases. The systematic name of this enzyme class is undecaprenyldiphospho-(N-acetyl-D-glucosaminyl-(1->4)-(N-acetyl-D-mu ramoylpentapeptide):undecaprenyldiphospho-(N-acetyl-D-glucosaminyl-( 1->4)-N-acetyl-D-muramoylpentapeptide) disaccharidetransferase. Other names in common use include PG-II, bactoprenyldiphospho-N-acetylmuramoyl-(N-acetyl-D-glucosaminyl)-, pentapeptide:peptidoglycan, N-acetylmuramoyl-N-acetyl-D-glucosaminyltransferase, penicillin binding protein (3 or 1B), and peptidoglycan transglycosylase. This enzyme participates in peptidoglycan biosynthesis.

Structural studies

As of late 2007, 3 structures have been solved for this class of enzymes, with PDB accession codes {{PDB link|2BG1}}, {{PDB link|2UWX}}, and {{PDB link|2UWY}}.

References

{{cite journal | vauthors = Taku A, Stuckey M, Fan DP | date = 1982 | title = Purification of the peptidoglycan transglycosylase of Bacillus megaterium | journal = J. Biol. Chem. | volume = 257 | pages = 5018–22 | pmid = 6802846 | issue = 9 }}
{{cite journal | vauthors = Goffin C, Ghuysen JM | date = 1998 | title = Multimodular penicillin-binding proteins: an enigmatic family of orthologs and paralogs | journal = Microbiol. Mol. Biol. Rev. | volume = 62 | pages = 1079–93 | pmid = 9841666 | issue = 4 | pmc = 98940 }}
{{cite journal | author = van Heijenoort J | date = 2001 | title = Formation of the glycan chains in the synthesis of bacterial peptidoglycan | journal = Glycobiology | volume = 11 | pages = 25R–36R | pmid = 11320055 | doi = 10.1093/glycob/11.3.25R | issue = 3 }}

2 : EC 2.4.1|Enzymes of known structure

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