Yes, the pH optimum of a reaction can be changed with a mutation of one
of the catalytic residue or with a neighboring non-catalytic residue. A
classic example is the K166R mutation of mandelate racemase.
see: Biochemistry. 1995 Mar 7;34(9):2788-97
https://www.ncbi.nlm.nih.gov/pubme
Hi,
apart from the possibilities of conformational flexibility affected by crystal
packing, just wondering if this mutation is supposed to actually cause an
increase or decrease in the corresponding activity (outside the context of a
crystal)? k(cat) and K(M) measured in solution would help her
letin board [mailto:CCP4BB@JISCMAIL.AC.UK
> ] On Behalf Of Pierre Nioche
> Sent: Thursday, April 13, 2017 11:28 AM
> To: CCP4BB@JISCMAIL.AC.UK
> Subject: [ccp4bb] in crystallo enzymatic activity
>
> Dear CCP4bb,
>
> We work on an enzyme that we crystallized with two s
irology
> University of Maryland, Baltimore
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>
> -Original Message-
> From: CCP4 bulletin board [mailto:CCP4BB@JISCMAIL.AC.UK] On Behalf Of Pierre
> Nioche
> Sent:
Behalf Of Pierre
Nioche
Sent: Thursday, April 13, 2017 11:28 AM
To: CCP4BB@JISCMAIL.AC.UK
Subject: [ccp4bb] in crystallo enzymatic activity
Dear CCP4bb,
We work on an enzyme that we crystallized with two substrates bound in the
active site (the reaction transform two substrates into two products
Dear CCP4bb,
We work on an enzyme that we crystallized with two substrates bound in
the active site (the reaction transform two substrates into two
products). We have also the structure with the two products. We are
able to see densities for the substrates when we collect data at
differen
