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Information on EC 2.8.1.10 - thiazole synthase and Organism(s) Saccharomyces cerevisiae and UniProt Accession P32318

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EC Tree
     2 Transferases
         2.8 Transferring sulfur-containing groups
             2.8.1 Sulfurtransferases
                2.8.1.10 thiazole synthase
IUBMB Comments
H2S can provide the sulfur in vitro. Part of the pathway for thiamine biosynthesis.
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Saccharomyces cerevisiae
UNIPROT: P32318
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The taxonomic range for the selected organisms is: Saccharomyces cerevisiae
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Synonyms
thiazole synthase, thiamine thiazole synthase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
1-deoxy-D-xylulose 5-phosphate + 2-iminoacetate + thiocarboxy-[sulfur-carrier protein ThiS] = 2-[(2R,5Z)-2-carboxy-4-methylthiazol-5(2H)-ylidene]ethyl phosphate + [sulfur-carrier protein ThiS] + 2 H2O
show the reaction diagram
the cofactor nicotinamide adenine dinucleotide is converted into adenosine diphospho-5-(beta-ethyl)-4-methylthiazole-2-carboxylic acid. The ADT ligand is tightly bound and can be released in vitro only upon protein denaturation. In this mechanism, cleavage of the N-glycosyl bond of NAD gives ADP-ribose.The first step in thiazole formation is similar to the chemistry used in ADP ribosylation
1-deoxy-D-xylulose 5-phosphate + 2-iminoacetate + thiocarboxy-[sulfur-carrier protein ThiS] = 2-[(2R,5Z)-2-carboxy-4-methylthiazol-5(2H)-ylidene]ethyl phosphate + [sulfur-carrier protein ThiS] + 2 H2O
show the reaction diagram
final step of the thiamin-thiazole biosynthesis is the concersion of a labile adenylated thiazole tautomer to the adenylated thiazole product. The conversion has an absolute requirement for enzyme catalysis
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PATHWAY SOURCE
PATHWAYS
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SYSTEMATIC NAME
IUBMB Comments
1-deoxy-D-xylulose 5-phosphate:thiol sulfurtransferase
H2S can provide the sulfur in vitro. Part of the pathway for thiamine biosynthesis.
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
1-deoxy-D-xylulose 5-phosphate + 2-iminoacetate + thiocarboxy-adenylate-[sulfur-carrier protein ThiS]
2-[(2R,5Z)-2-carboxy-4-methylthiazol-5(2H)-ylidene]ethyl phosphate + [sulfur-carrier protein ThiS] + 2 H2O
show the reaction diagram
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additional information
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
1-deoxy-D-xylulose 5-phosphate + 2-iminoacetate + thiocarboxy-adenylate-[sulfur-carrier protein ThiS]
2-[(2R,5Z)-2-carboxy-4-methylthiazol-5(2H)-ylidene]ethyl phosphate + [sulfur-carrier protein ThiS] + 2 H2O
show the reaction diagram
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
34991
x * 34991, calculated
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
x * 34991, calculated
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
C205S variant with a bound glycine imine intermediate, hanging drop vapor diffusion method, using 25% (w/v) PEG1500, 0.0125 M succinic acid, 0.044 M sodium dihydrogen phosphate, and 0.044 M glycine, pH 8.5
native protein to 1.8 A resolution. Thi4 exists as an homooctamer with the disordered and largely hydrophilic N-terminal regions located on the exterior of the molecule. The octamer has the shape of a ring with flattened sides. Adenosine diphospho-5-(beta-ethyl)-4-methylthiazole-2-carboxylic acid is bound to the Thi4 active site, which is located near the inner ring of the octameric complex.. NAD is the most likely precursor
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
Ni-NTA column chromatography and Superdex 200 gel filtration
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli BL21(DE3) cells
expression in Escherichia coli
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Jurgenson, C.T.; Chatterjee, A.; Begley, T.P.; Ealick, S.E.
Structural insights into the function of the thiamin biosynthetic enzyme Thi4 from Saccharomyces cerevisiae
Biochemistry
45
11061-11070
2006
Saccharomyces cerevisiae (P32318), Saccharomyces cerevisiae
Manually annotated by BRENDA team
Chatterjee, A.; Schroeder, F.C.; Jurgenson, C.T.; Ealick, S.E.; Begley, T.P.
Biosynthesis of the thiamin-thiazole in eukaryotes: identification of a thiazole tautomer intermediate
J. Am. Chem. Soc.
130
11394-11398
2008
Saccharomyces cerevisiae
Manually annotated by BRENDA team
Chatterjee, A.; Abeydeera, N.D.; Bale, S.; Pai, P.J.; Dorrestein, P.C.; Russell, D.H.; Ealick, S.E.; Begley, T.P.
Saccharomyces cerevisiae THI4p is a suicide thiamine thiazole synthase
Nature
478
542-546
2011
Saccharomyces cerevisiae (P32318), Saccharomyces cerevisiae
Manually annotated by BRENDA team
Zhang, X.; Eser, B.E.; Chanani, P.K.; Begley, T.P.; Ealick, S.E.
Structural Basis for iron-mediated sulfur transfer in archael and yeast thiazole synthases
Biochemistry
55
1826-1838
2016
Methanocaldococcus jannaschii, Methanotorris igneus, Saccharomyces cerevisiae (P32318)
Manually annotated by BRENDA team