Enzymes
UniProtKB help_outline | 1 proteins |
Enzyme class help_outline |
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GO Molecular Function help_outline |
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Reaction participants Show >> << Hide
- Name help_outline pyridine Identifier CHEBI:16227 (Beilstein: 103233; CAS: 110-86-1) help_outline Charge 0 Formula C5H5N InChIKeyhelp_outline JUJWROOIHBZHMG-UHFFFAOYSA-N SMILEShelp_outline c1ccncc1 2D coordinates Mol file for the small molecule Search links Involved in 3 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline thiamine Identifier CHEBI:18385 (Beilstein: 3595616; CAS: 70-16-6) help_outline Charge 1 Formula C12H17N4OS InChIKeyhelp_outline JZRWCGZRTZMZEH-UHFFFAOYSA-N SMILEShelp_outline CC1=C(CCO)SC=[N+]1CC1=CN=C(C)N=C1N 2D coordinates Mol file for the small molecule Search links Involved in 9 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline 5-(2-hydroxyethyl)-4-methylthiazole Identifier CHEBI:17957 (CAS: 137-00-8) help_outline Charge 0 Formula C6H9NOS InChIKeyhelp_outline BKAWJIRCKVUVED-UHFFFAOYSA-N SMILEShelp_outline Cc1ncsc1CCO 2D coordinates Mol file for the small molecule Search links Involved in 3 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline heteropyrithiamine Identifier CHEBI:11222 Charge 1 Formula C11H13N4 InChIKeyhelp_outline SPQICHFDXHERAC-UHFFFAOYSA-N SMILEShelp_outline Cc1ncc(C[n+]2ccccc2)c(N)n1 2D coordinates Mol file for the small molecule Search links Involved in 1 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
Cross-references
RHEA:17697 | RHEA:17698 | RHEA:17699 | RHEA:17700 | |
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Reaction direction help_outline | undefined | left-to-right | right-to-left | bidirectional |
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Publications
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The extracellular thiaminase I of Bacillus thiaminolyticus. I. Purification and physicochemical properties.
Wittliff J.L., Airth R.L.
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Crystal structure of thiaminase-I from Bacillus thiaminolyticus at 2.0-A resolution.
Campobasso N., Costello C.A., Kinsland C., Begley T.P., Ealick S.E.
Thiaminase-I catalyzes the replacement of the thiazole moiety of thiamin with a wide variety of nucleophiles, such as pyridine, aniline, catechols, quinoline, and cysteine. The crystal structure of the enzyme from Bacillus thiaminolyticus was determined at 2.5 A resolution by multiple isomorphous ... >> More
Thiaminase-I catalyzes the replacement of the thiazole moiety of thiamin with a wide variety of nucleophiles, such as pyridine, aniline, catechols, quinoline, and cysteine. The crystal structure of the enzyme from Bacillus thiaminolyticus was determined at 2.5 A resolution by multiple isomorphous replacement and refined to an R factor of 0.195 (Rfree = 0.272). Two other structures, one native and one containing a covalently bound inhibitor, were determined at 2.0 A resolution by molecular replacement from a second crystal form and were refined to R factors of 0.205 and 0.217 (Rfree = 0.255 and 0.263), respectively. The overall structure contains two alpha/beta-type domains separated by a large cleft. At the base of the cleft lies Cys113, previously identified as a key active site nucleophile. The structure with a covalently bound thiamin analogue, which functions as a mechanism-based inactivating agent, confirms the location of the active site. Glu241 appears to function as an active site base to increase the nucleophilicity of Cys113. The mutant Glu241Gln was made and shows no activity. Thiaminase-I shows no sequence identity to other proteins in the sequence databases, but the three-dimensional structure shows very high structural homology to the periplasmic binding proteins and the transferrins. << Less