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Information on EC 4.1.99.19 - 2-iminoacetate synthase and Organism(s) Escherichia coli and UniProt Accession P30140

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EC Tree
     4 Lyases
         4.1 Carbon-carbon lyases
             4.1.99 Other carbon-carbon lyases
                4.1.99.19 2-iminoacetate synthase
IUBMB Comments
Binds a [4Fe-4S] cluster that is coordinated by 3 cysteines and an exchangeable S-adenosyl-L-methionine molecule. The first stage of catalysis is reduction of the S-adenosyl-L-methionine to produce methionine and a 5-deoxyadenosin-5-yl radical that is crucial for the conversion of the substrate. The reductant is assumed to be NADPH, which is provided by a flavoprotein:NADPH oxidoreductase system . Part of the pathway for thiamine biosynthesis.
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This record set is specific for:
Escherichia coli
UNIPROT: P30140
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The taxonomic range for the selected organisms is: Escherichia coli
The expected taxonomic range for this enzyme is: Bacteria, Archaea
Synonyms
thiH, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
thiH
-
-
-
-
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
L-tyrosine + S-adenosyl-L-methionine + NADPH = 2-iminoacetate + 4-methylphenol + 5'-deoxyadenosine + L-methionine + NADP+ + H+
show the reaction diagram
ThiH is a member of the radical-S-adenosyl-L-methionine family. Proposed mechanism of ThiH-dependent cleavage of L-tyrosine: S-adenosyl-L-methionine is reductively cleaved to yield a highly reactive 5'-deoxyadenosyl radical. This radical is proposed to abstract the phenolic hydrogen atom from tyrosine, and the resultant substrate radical cleaves to yield dehydroglycine, which is required by ThiG for the thiazole cyclization reaction
PATHWAY SOURCE
PATHWAYS
-
-
SYSTEMATIC NAME
IUBMB Comments
L-tyrosine 4-methylphenol-lyase (2-iminoacetate-forming)
Binds a [4Fe-4S] cluster that is coordinated by 3 cysteines and an exchangeable S-adenosyl-L-methionine molecule. The first stage of catalysis is reduction of the S-adenosyl-L-methionine to produce methionine and a 5-deoxyadenosin-5-yl radical that is crucial for the conversion of the substrate. The reductant is assumed to be NADPH, which is provided by a flavoprotein:NADPH oxidoreductase system [4]. 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
L-tyrosine + S-adenosyl-L-methionine + reduced acceptor
2-iminoacetate + 4-methylphenol + 5'-deoxyadenosine + L-methionine + acceptor + 2 H+
show the reaction diagram
the reductive cleavage of S-adenosyl-L-methionine yields the highly reactive 5'-deoxyadenosyl radical, which can abstract the phenolic hydrogen atom from tyrosine
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-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
[4Fe-4S]-center
essential for activity
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4Fe-4S cluster
-
4Fe-4S-center
-
Iron
iron content is 5.2 mol eq of iron per mol of ThiH, contains an 4F-4S cluster essential for activity
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
physiological function
-
the enzyme complex ThiGH is involved in the rate-limiting step of thiamine biosynthesis
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
44143
additional information
the 440000 Da complex contains both ThiG and ThiH-His
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
when isolated under anaerobic conditions, ThiG and ThiH-His co-purify as a large multimeric non-covalent complex
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
C-terminally hexahistidine-tagged ThiH(ThiH-His) is expressed in Escherichia coli as a soluble protein from thiGHHis-tag and thiFSGH-His-tag-bearing plasmids
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Kriek, M.; Martins, F.; Challand, M.R.; Croft, A.; Roach, P.L.
Thiamine biosynthesis in Escherichia coli: identification of the intermediate and by-product derived from tyrosine
Angew. Chem. Int. Ed. Engl.
46
9223-9226
2007
Escherichia coli (P30140)
Manually annotated by BRENDA team
Leonardi, R.; Fairhurst, S.A.; Kriek, M.; Lowe, D.J.; Roach, P.L.
Thiamine biosynthesis in Escherichia coli: isolation and initial characterisation of the ThiGH complex
FEBS Lett.
539
95-99
2003
Escherichia coli (P30140)
Manually annotated by BRENDA team
Leonardi, R.; Roach, P.L.
Thiamine biosynthesis in Escherichia coli: in vitro reconstitution of the thiazole synthase activity
J. Biol. Chem.
279
17054-17062
2004
Escherichia coli
Manually annotated by BRENDA team
Kriek, M.; Martins, F.; Leonardi, R.; Fairhurst, S.A.; Lowe, D.J.; Roach, P.L.
Thiazole synthase from Escherichia coli: an investigation of the substrates and purified proteins required for activity in vitro
J. Biol. Chem.
282
17413-17423
2007
Escherichia coli (P30140)
Manually annotated by BRENDA team