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Information on EC 2.4.2.54 - beta-ribofuranosylphenol 5'-phosphate synthase and Organism(s) Methanocaldococcus jannaschii and UniProt Accession Q58822

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EC Tree
     2 Transferases
         2.4 Glycosyltransferases
             2.4.2 Pentosyltransferases
                2.4.2.54 beta-ribofuranosylphenol 5'-phosphate synthase
IUBMB Comments
The enzyme is involved in biosynthesis of tetrahydromethanopterin in archaea. It can utilize both 4-hydroxybenzoate and 4-aminobenzoate as substrates, but only the former is known to be produced by methanogenic archaea . The activity is dependent on Mg2+ or Mn2+ .
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Methanocaldococcus jannaschii
UNIPROT: Q58822
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Word Map
The taxonomic range for the selected organisms is: Methanocaldococcus jannaschii
The expected taxonomic range for this enzyme is: Archaea, Bacteria
Synonyms
rfap synthase, beta-rfap synthase, beta-rfa-p synthase, ribofuranosylaminobenzene 5'-phosphate synthase, beta-ribofuranosylaminobenzene 5'-phosphate synthase, mth0830, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
beta-ribofuranosylhydroxybenzene 5'-phosphate synthase
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PATHWAY SOURCE
PATHWAYS
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SYSTEMATIC NAME
IUBMB Comments
5-phospho-alpha-D-ribose 1-diphosphate:4-hydroxybenzoate 5-phospho-beta-D-ribofuranosyltransferase (decarboxylating)
The enzyme is involved in biosynthesis of tetrahydromethanopterin in archaea. It can utilize both 4-hydroxybenzoate and 4-aminobenzoate as substrates, but only the former is known to be produced by methanogenic archaea [4]. The activity is dependent on Mg2+ or Mn2+ [1].
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
5-phospho-alpha-D-ribose 1-diphosphate + 4-aminobenzoate
4-(beta-D-ribofuranosyl)aminobenzene 5'-phosphate + CO2 + diphosphate
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
5-phospho-alpha-D-ribose 1-diphosphate + 4-aminobenzoate
4-(beta-D-ribofuranosyl)aminobenzene 5'-phosphate + CO2 + diphosphate
show the reaction diagram
the enzyme is involved in biosynthesis of tetrahydromethanopterin, a folate analog involved in the C1 metabolism of methanogenic archaea, sulfate-reducing archaea, and methylotrophic bacteria
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
4-(beta-D-ribofuranosyl)aminobenzene 5'-phosphate
uncompetitive inhibition under varied 5-phospho-alpha-D-ribose 1-diphosphate and saturated 4-aminobenzoate or under varied 4-aminobenzoate and saturated 5-phospho-alpha-D-ribose 1-diphosphate
CO2
uncompetitive inhibition under varied 5-phospho-alpha-D-ribose 1-diphosphate and saturated 4-aminobenzoate. Mixed type of inhibition under varied 4-aminobenzoate and saturated 5-phospho-alpha-D-ribose 1-diphosphate
diphosphate
competitive inhibition under saturated 5-phospho-alpha-D-ribose 1-diphosphate and varied 4-aminobenzoate. Mixed type of inhibition under varied 4-aminobenzoate and saturated 5-phospho-alpha-D-ribose 1-diphosphate
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.15
4-Aminobenzoate
pH 4.8, 70°C
1.5
5-phospho-alpha-D-ribose 1-diphosphate
pH 4.8, 70°C
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.23
5-phospho-alpha-D-ribose 1-diphosphate
pH 4.8, 70°C
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.21 - 0.3
4-(beta-D-ribofuranosyl)aminobenzene 5'-phosphate
0.99
CO2
pH 4.8, 70°C, uncompetitive inhibition under varied 5-phospho-alpha-D-ribose 1-diphosphate and saturated 4-aminobenzoate
0.32
diphosphate
pH 4.8, 70°C, competitive inhibition under saturated 5-phospho-alpha-D-ribose 1-diphosphate and varied 4-aminobenzoate
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
36200
2 * 36200, SDS-PAGE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
homodimer
2 * 36200, SDS-PAGE
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
overexpression in Escherichia coli
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Dumitru, R.V.; Ragsdale, S.W.
Mechanism of 4-(beta-D-ribofuranosyl)aminobenzene 5'-phosphate synthase, a key enzyme in the methanopterin biosynthetic pathway
J. Biol. Chem.
279
39389-39395
2004
Methanocaldococcus jannaschii (Q58822), Methanocaldococcus jannaschii
Manually annotated by BRENDA team