Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 2.3.1.201 extracted from

  • Ma, G.; Cheng, N.; Su, H.; Liu, Y.
    Exploring the substrate-assisted acetylation mechanism by UDP-linked sugar N-acetyltransferase from QM/MM calculations: The role of residue Asn84 and the effects of starting geometries (2015), RSC Adv., 5, 7781-7788.
No PubMed abstract available

Crystallization (Commentary)

Crystallization (Comment) Organism
QM/MM calculations reveal two sequential steps in the catalyzation process. The nucleophilic attack of the C3-amino group of the substrate on the carbonyl carbon of acetyl-CoA occurs in concert with the departure of CoA from acetyl-CoA, generating a negatively charged CoA and a positively charged intermediate. Subsequently, the sulfur anion of CoA accepts the proton of the positively charged intermediate to yield the final product. Asn84 is important for promoting the catalysis by forming a hydrogen bond with the C3-amino group to position the lone pair of the electrons of the C3-amino group in an ideal orientation for nucleophilic attack and stabilize the transition states and intermediate Bordetella petrii

Organism

Organism UniProt Comment Textmining
Bordetella petrii A9IH93
-
-
Bordetella petrii DSM 12804 A9IH93
-
-