Journal
BIOCHEMISTRY
Volume 45, Issue 16, Pages 5122-5128Publisher
AMER CHEMICAL SOC
DOI: 10.1021/bi052403n
Keywords
-
Categories
Funding
- NHLBI NIH HHS [HL52622, R01 HL062244, R01 HL052622, HL62244, R01 HL062244-05A1, R01 HL052622-09, R01 HL062244-06] Funding Source: Medline
- NIAID NIH HHS [R01 AI050050, AI 50050] Funding Source: Medline
- NIGMS NIH HHS [R01 GM038060-18, R01 GM038060-17, GM38060, R01 GM038060] Funding Source: Medline
Ask authors/readers for more resources
The 3-O-sulfonation of glucosamine residues in heparan sulfate (HS) by 3-O-sulfotransferase (3-OST) is a key substitution that is present in HS sequences of biological importance, in particular HS anticoagulant activity. Six different isoforms of 3-OST have been identified that exhibit different substrate specificity. In this paper the affinity and kinetics of the interaction between 3-O-sulfotransferase isoform 1 (3-OST-1) and HS have been examined using surface plasmon resonance (SPR). 3-OST-1 binds with micomolar affinity to HS (K-D = 2.79 mu M), and this interaction is apparently independent of the presence of the coenzyme, 3'-phosphoadenosine 5'-phosphosulfate (PAPS). A conformational change in the complex has also been detected, supporting data from previous studies. Selected 3-OST-1 mutants have provided valuable information of amino acid residues that participate in 3-OST-1 interaction with HS substrate and its catalytic activity. The results from this study contribute to understanding the substrate specificity among, the 3-OST isoforms and in the mechanism of 3-OST-1-catalyzed biosynthesis of anticoagulant HS.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available