Any feedback?
Please rate this page
(enzyme.php)
(0/150)

BRENDA support

BRENDA Home
show all | hide all No of entries

Information on EC 2.4.2.60 - cysteine-dependent adenosine diphosphate thiazole synthase and Organism(s) Methanocaldococcus jannaschii and UniProt Accession Q58018

for references in articles please use BRENDA:EC2.4.2.60
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
IUBMB Comments
This iron dependent enzyme, found in fungi, plants, and some archaea, is involved in the thiamine phosphate biosynthesis pathway. It is a single turn-over enzyme since the cysteine residue is not regenerated in vivo . The homologous enzyme in archaea (EC 2.4.2.59, sulfide-dependent adenosine diphosphate thiazole synthase) uses sulfide as sulfur donor.
Specify your search results
Select one or more organisms in this record: ?
This record set is specific for:
Methanocaldococcus jannaschii
UNIPROT: Q58018
Show additional data
Do not include text mining results
Include (text mining) results
Include results (AMENDA + additional results, but less precise)
The taxonomic range for the selected organisms is: Methanocaldococcus jannaschii
The expected taxonomic range for this enzyme is: Eukaryota, Archaea
Reaction Schemes
hide
NAD+
+
glycine
+
[ADP-thiazole synthase]-L-cysteine
=
nicotinamide
+
ADP-5-ethyl-4-methylthiazole-2-carboxylate
+
[ADP-thiazole synthase]-dehydroalanine
+
3
H2O
+
+
[ADP-thiazole synthase]-L-cysteine
=
+
+
[ADP-thiazole synthase]-dehydroalanine
+
3
Synonyms
cypbp37, thi-4, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ADP-thiazole synthase
-
-
-
-
THI1
-
-
-
-
PATHWAY SOURCE
PATHWAYS
-
-
SYSTEMATIC NAME
IUBMB Comments
NAD+:glycine ADP-D-ribosyltransferase (dehydroalanine-producing)
This iron dependent enzyme, found in fungi, plants, and some archaea, is involved in the thiamine phosphate biosynthesis pathway. It is a single turn-over enzyme since the cysteine residue is not regenerated in vivo [3]. The homologous enzyme in archaea (EC 2.4.2.59, sulfide-dependent adenosine diphosphate thiazole synthase) uses sulfide as sulfur donor.
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in ERscherichia 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 igneus, Methanocaldococcus jannaschii (Q58018), Methanocaldococcus jannaschii DSM 2661 (Q58018), Saccharomyces cerevisiae, Saccharomyces cerevisiae (P32318), Saccharomyces cerevisiae ATCC 204508 (P32318)
Manually annotated by BRENDA team