EC Number   |
Reaction |
Reference |
|---|
    5.1.3.3 | alpha-D-glucose = beta-D-glucose |
concerted general acid/general base mechanism |
661052 |
| 5.1.3.3 | alpha-D-glucose = beta-D-glucose |
E307 and H176 may act as catalytic acid and catalytic base, respectively |
662224 |
| 5.1.3.3 | alpha-D-glucose = beta-D-glucose |
mechanism, one of the catalytic groups H104, H175, or E309, shuttles a proton to and from the endocyclic oxygen and the other two shuttle protons to the anomeric oxygen atoms. Ring opening of alpha-D-glucose limits the rate at low pH, but ring closure does not become rate limiting at pH up to 8.5 |
661071 |
| 5.1.3.3 | alpha-D-glucose = beta-D-glucose |
reaction mechanism does not involve dehydration, any dehydrogenation reaction on carbon-bound hydrogen, or the hydrated derivative of glucose aldehyde, nor is a single displacement mechanism involved. The enzyme-catalyzed mutarotation is essentially similar to the spontaneous or acid catalyzed process. Mutarotase is an enzyme with a proton-transferring function #2# |
2363 |
| 5.1.3.3 | alpha-D-glucose = beta-D-glucose |
residues E304 and H170 are critical for catalysis and H96 and D243 are important for substrate positioning |
663325 |
| 5.1.3.3 | alpha-D-glucose = beta-D-glucose |
residues responsible for anchoring the sugar include R71, H96, H170, D243 and E304. E304 may act as general acid/base |
662113 |
| 5.1.3.3 | alpha-D-glucose = beta-D-glucose |
the mechanism of the enzymatically catalyzed mutarotation is basically different from that of the nonenzymatically catalyzed mutarotation. The mutarotase acts primarily as a base catalyst. The enzymatically catalyzed mutarotation proceeds via the acyclic aldehyde form of the aldose |
2364 |
| 5.1.3.3 | alpha-D-glucose = beta-D-glucose |
Trp is involved as glucose-binding site and catalysis of the mutarotation reaction is accomplished by a ring-distortion type of mechanism |
2366 |
