Information on EC 2.4.2.60 - cysteine-dependent adenosine diphosphate thiazole synthase

for references in articles please use BRENDA:EC2.4.2.60
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The expected taxonomic range for this enzyme is: Eukaryota, Archaea

EC NUMBER
COMMENTARY hide
2.4.2.60
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RECOMMENDED NAME
GeneOntology No.
cysteine-dependent adenosine diphosphate thiazole synthase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
NAD+ + glycine + [ADP-thiazole synthase]-L-cysteine = nicotinamide + ADP-5-ethyl-4-methylthiazole-2-carboxylate + [ADP-thiazole synthase]-dehydroalanine + 3 H2O
show the reaction diagram
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
thiazole biosynthesis III (eukaryotes)
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Thiamine metabolism
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Metabolic pathways
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SYSTEMATIC NAME
IUBMB Comments
NAD+:glycine ADP-D-ribosyltransferase (dehydroalanine-producing)
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
NAD+ + glycine + [ADP-thiazole synthase]-L-cysteine
nicotinamide + ADP-5-ethyl-4-methylthiazole-2-carboxylate + [ADP-thiazole synthase]-dehydroalanine + 3 H2O
show the reaction diagram
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?
additional information
?
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NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
NAD+ + glycine + [ADP-thiazole synthase]-L-cysteine
nicotinamide + ADP-5-ethyl-4-methylthiazole-2-carboxylate + [ADP-thiazole synthase]-dehydroalanine + 3 H2O
show the reaction diagram
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?
additional information
?
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Thi4 is a suicidal enzyme undergoing only a single turnover
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
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high level of expression
Manually annotated by BRENDA team
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high level of expression in chloroplast-containing parenchymatic cells of leaves
Manually annotated by BRENDA team
high level expression in actinorhizal nodule, high levels of Thi1 mRNA in the infected cortical cells and in the pericycle of the nodule vascular system
Manually annotated by BRENDA team
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lower level of expression
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
191000
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gel filtration, wild-type
203000
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gel filtration, mutant A140V
241940
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mass spectrometry, wild-type
242290
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mass spectrometry, mutant A140V
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
octamer
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8 * 36600, calculated
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
to 1.6 A resolution, enzyme contains bound 2-carboxylate-4-methyl-5-beta-(ethyl adenosine 5'-diphosphate) thiazole
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structure with bound glycine imine intermediate and iron. The Thi4 orthologs from Methanocaldococcus jannaschii and Methanocaldococcus igneus are structurally similar to Thi4 from Saccharomyces cerevisiae. All active site residues are conserved except for a key cysteine residue, which in Saccharomyces cerevisiae is the source of the thiazole sulfur atom
Methanocaldococcus igneus
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structure in complex with ADP-ribulose. The Thi4 orthologs from Methanocaldococcus jannaschii and Methanocaldococcus igneus are structurally similar to Thi4 from Saccharomyces cerevisiae. All active site residues are conserved except for a key cysteine residue, which in Saccharomyces cerevisiae is the source of the thiazole sulfur atom
structure of mutant C205S with a bound glycine imine intermediate. Comparison with structures of Methanococcus jannaschii and Methanococcus igneus homologues
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to 1.8 A resolution. Thi4 exists as an octamer with two monomers in the asymmetric unit. A tightly bound adenosine diphospho-5-(beta-ethyl)-4-methylthiazole-2-carboxylic acid is present at the active site. The Thi4 structure reveals a protein structure with a GR2 domain that binds NAD instead of FAD
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
56
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mutant A140V, beginning of thermal denaturation
60
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wild-type, beginning of thermal denaturation
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
recombinant protein
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expression in ERscherichia coli
expression in Escherichia coli
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
expression is completely repressed throughout batch culture by thiamine at a concentration around 1 microM, but high level constitutive expression occurs in thiamine-free medium
expression is induced by osmotic stress, salinity stress and oxidative stress
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expression is induced by stress
expression is induced by to oxidative and osmotic stress
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expression is induced when the intracellular concentration of thiamine falls to 20 pmol per 10 million cells
presence of thiamine does not suppress expression
the expression of CyPBP37 is repressed by thiamine but not by thiazole in the growth medium
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
D33G
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no significant effect on activity
D41G
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no significant effect on activity
E222G
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complete loss of activity, leading to disruption of the thiamine biosynthetic route
G77V
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complete loss of activity, leading to disruption of the thiamine biosynthetic route
H167F
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complete loss of activity, leading to disruption of the thiamine biosynthetic route
K128M
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no significant effect on activity
W80L
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no significant effect on activity
R301Q
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inactive