Talk:Glycoside Hydrolase Family 3

Comment from Brian Mark, April 2013

The GH3 page has received a comprehensive update. The following comments have been addressed. Thank-you for the input!

Comment from Shinya Fushinobu, Sept. 2011

Litzinger et al. (2010) suggested that the acid/base catalyst of 2 domain NagZs (and also 1 domain NagZs) is an Asp-His dyad in the (β/α)₈ domain. pmid: 20826810.

Update to Catalytic Residues section needed?

Given the growing amount of information about the identity of the GH3 catalytic residues - and in particular the acid/base - in different enzymes/subfamilies, I wonder if a update of this section isn't needed?

Here are some key acid/base ID references [1, 2, 3, 4, 5, 6, 7, 8, 9], one of which also confirms the catalytic nucleophile [7]. These references are nucleophile-specific studies [10, 11]:

References

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1. Subfamily 4, 3-D homology model, mutagenesis, kinetic analysis, pH profile, azide rescue

2. 1-domain Nag, experimental structure, ligand complex, mobile loop bearing acid/base

3. 2-domain Nag, strucuture, mutagenesis, kinetic analysis, pH profile, azide rescue unsuccessful

4. Subfamily 5, experimental structure, complexes, reduced Km for mutant with PNP-Glc

5. Subfamily 5, experimental structure, product complex

6. Nag - relevant? Appears to be mis-identification.

7. Subfamily 5, kinetic analysis, pH profile, azide rescue

8. Subfamily 5, Glu-473 labelled by N-bromoacetyl-beta-d-glucosylamine

9. Subfamily 5, kinetic analysis, pH profile, azide rescue

Harry Brumer (talk) 17:55, 14 December 2012 (PST)