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Information on EC 4.2.1.151 - chorismate dehydratase and Organism(s) Thermus thermophilus and UniProt Accession Q5SK49

for references in articles please use BRENDA:EC4.2.1.151
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EC Tree
     4 Lyases
         4.2 Carbon-oxygen lyases
             4.2.1 Hydro-lyases
                4.2.1.151 chorismate dehydratase
IUBMB Comments
The enzyme, found in several bacterial species, is part of the futalosine pathway for menaquinone biosynthesis.
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Select one or more organisms in this record: ?
This record set is specific for:
Thermus thermophilus
UNIPROT: Q5SK49
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The taxonomic range for the selected organisms is: Thermus thermophilus
The expected taxonomic range for this enzyme is: Bacteria, Archaea
Synonyms
chorismate dehydratase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TTHA0803
locus name
SYSTEMATIC NAME
IUBMB Comments
chorismate hydro-lyase (3-[(1-carboxyvinyl)oxy]benzoate-forming)
The enzyme, found in several bacterial species, is part of the futalosine pathway for menaquinone biosynthesis.
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
chorismate
3-[(1-carboxyvinyl)oxy]benzoate + 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
chorismate
3-[(1-carboxyvinyl)oxy]benzoate + H2O
show the reaction diagram
the enzyme is part of the futalosine pathway for menaquinone biosynthesis
-
-
?
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.162
chorismate
pH and temperature not specified in the publication
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1.27
chorismate
pH and temperature not specified in the publication
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
7.8
chorismate
pH and temperature not specified in the publication
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
SwissProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
the enzyme is part of the futalosine pathway for menaquinone biosynthesis
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
30500
x * 30500, SDS-PAGE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
x * 30500, SDS-PAGE
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
overexpression in Escherichia coli BL21 (DE3)
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Mahanta, N.; Fedoseyenko, D.; Dairi, T.; Begley, T.P.
Menaquinone biosynthesis: formation of aminofutalosine requires a unique radical SAM enzyme
J. Am. Chem. Soc.
135
15318-15321
2013
Thermus thermophilus (Q5SK49), Thermus thermophilus HB8 / ATCC 27634 / DSM 579 (Q5SK49)
Manually annotated by BRENDA team