2001
DOI: 10.1038/35090602
|View full text |Cite
|
Sign up to set email alerts
|

Catalysis by hen egg-white lysozyme proceeds via a covalent intermediate

Abstract: Hen egg-white lysozyme (HEWL) was the first enzyme to have its three-dimensional structure determined by X-ray diffraction techniques. A catalytic mechanism, featuring a long-lived oxocarbenium-ion intermediate, was proposed on the basis of model-building studies. The 'Phillips' mechanism is widely held as the paradigm for the catalytic mechanism of beta-glycosidases that cleave glycosidic linkages with net retention of configuration of the anomeric centre. Studies with other retaining beta-glycosidases, howev… Show more

Help me understand this report

Search citation statements

Order By: Relevance

Paper Sections

Select...
3
1

Citation Types

17
469
1
4

Year Published

2003
2003
2017
2017

Publication Types

Select...
5
4

Relationship

0
9

Authors

Journals

citations
Cited by 595 publications
(491 citation statements)
references
References 29 publications
17
469
1
4
Order By: Relevance
“…For inverting glycosidases and glycosyltransferases, the proposed single displacement mechanism is well established (50). There is also structural and kinetic evidence that retaining glycosidases follow a double displacement mechanism with participation of a covalent enzyme-substrate intermediate (49,51).…”
Section: Resultsmentioning
confidence: 92%
“…For inverting glycosidases and glycosyltransferases, the proposed single displacement mechanism is well established (50). There is also structural and kinetic evidence that retaining glycosidases follow a double displacement mechanism with participation of a covalent enzyme-substrate intermediate (49,51).…”
Section: Resultsmentioning
confidence: 92%
“…[37][38][39][40][41] The enzymes hydrolyse glycosidic bonds in these molecules by distorting the ring into a half-chair conformation. In this strained state the glycosidic bond is easily broken.…”
Section: Resultsmentioning
confidence: 99%
“…In this strained state the glycosidic bond is easily broken. 38,39,41 Therefore, the active site amino acids of the hen-egg lysozyme should interact with sugars, but this interaction will be optimised for a hydrolysis process rather than tight binding. It is interesting to note that the active site correspond to the only positive peaks in Fig.…”
Section: Resultsmentioning
confidence: 99%
“…Vocadlo et al (2001) concluded in their electrospray-ionization mass-spectrometric study that the catalytic mechanism of lysozyme involves an intermediate complex in which one sugar ring is covalently bonded to Asp52. A crystallographic study at 1.5 Å resolution of HEWL crystallized with substrate by Strynadka & James (1991) supports the Phillips mechanism (Phillips, 1966) and does not indicate a covalent intermediate.…”
Section: Introductionmentioning
confidence: 99%