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Information on EC 2.4.2.59 - sulfide-dependent adenosine diphosphate thiazole synthase and Organism(s) Methanocaldococcus jannaschii and UniProt Accession Q58018

for references in articles please use BRENDA:EC2.4.2.59
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IUBMB Comments
This iron dependent enzyme, found in most archaea, is involved in the biosynthesis of thiamine phosphate. The homologous enzyme from plants and fungi (EC 2.4.2.60, cysteine-dependent adenosine diphosphate thiazole synthase) uses an intrinsic cysteine as sulfur donor and, unlike the archaeal enzyme, is a single turn-over enzyme.
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Methanocaldococcus jannaschii
UNIPROT: Q58018
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The taxonomic range for the selected organisms is: Methanocaldococcus jannaschii
The expected taxonomic range for this enzyme is: Bacteria, Archaea, Eukaryota
Synonyms
MJ0601, Thi4, thiamine thiazole synthase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
PATHWAY SOURCE
PATHWAYS
-
-
SYSTEMATIC NAME
IUBMB Comments
NAD+:glycine ADP-D-ribosyltransferase (sulfide-adding)
This iron dependent enzyme, found in most archaea, is involved in the biosynthesis of thiamine phosphate. The homologous enzyme from plants and fungi (EC 2.4.2.60, cysteine-dependent adenosine diphosphate thiazole synthase) uses an intrinsic cysteine as sulfur donor and, unlike the archaeal enzyme, is a single turn-over enzyme.
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 + sulfide
nicotinamide + ADP-5-ethyl-4-methylthiazole-2-carboxylate + 3 H2O
show the reaction diagram
-
-
-
?
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
NAD+ + glycine + sulfide
nicotinamide + ADP-5-ethyl-4-methylthiazole-2-carboxylate + 3 H2O
show the reaction diagram
-
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Ca2+
may substitute for iron
Co2+
may substitute for iron
Fe3+
highest levels of activity in presence of FE2+ or Fe3+, iron is involved in sulfur transfer
Mg2+
may substitute for iron
Mn2+
may substitute for iron
Ni2+
may substitute for iron
Zn2+
may substitute for iron
additional information
Cu+ or Cu2+ do not support activity
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
enzyme complexed with ADP-ribulose, hanging drop vapor diffusion method, using 1.05 M potassium/sodium tartrate, 0.1 M CHES/sodium hydroxide, pH 9.5 and 0.2 M lithium sulfate
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Zhang, X.; Eser, B.; Chanani, P.; Begley, T.; Ealick, S.
Structural basis for iron-mediated sulfur transfer in archael and yeast thiazole synthases
Biochemistry
55
1826-1838
2016
Methanocaldococcus jannaschii (Q58018), Methanocaldococcus jannaschii ATCC 43067 (Q58018), Methanotorris igneus (F6BCS4)
Manually annotated by BRENDA team
Eser, B.; Zhang, X.; Chanani, P.; Begley, T.; Ealick, S.
From suicide enzyme to catalyst the iron-dependent sulfide transfer in Methanococcus jannaschii thiamin thiazole biosynthesis
J. Am. Chem. Soc.
138
3639-3642
2016
Methanocaldococcus jannaschii (Q58018), Methanocaldococcus jannaschii DSM 2661 (Q58018)
Manually annotated by BRENDA team