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Information on EC 6.3.2.34 - coenzyme F420-1:gamma-L-glutamate ligase and Organism(s) Methanocaldococcus jannaschii and UniProt Accession Q58178

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EC Tree
IUBMB Comments
This protein catalyses the successive addition of two glutamate residues to cofactor F420 by two distinct and independent reactions. In the first reaction (EC 6.3.2.31, coenzyme F420-0---L-glutamate ligase) the enzyme attaches a glutamate via its alpha-amine group to F420-0. In the second reaction, which is described here, the enzyme catalyses the addition of a second L-glutamate residue to the gamma-carboxyl of the first glutamate.
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Methanocaldococcus jannaschii
UNIPROT: Q58178
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The taxonomic range for the selected organisms is: Methanocaldococcus jannaschii
The expected taxonomic range for this enzyme is: Bacteria, Archaea
Synonyms
bifunctional F420 biosynthesis protein FbiB, BQ2027_MB3290, CofE, CofE-AF, F420-0:gamma-glutamyl ligase, F420:gamma-glutamyl ligase, FbiB, MJ0768, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
F420-0:gamma-glutamyl ligase
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SYSTEMATIC NAME
IUBMB Comments
L-glutamate:coenzyme F420-1 ligase (GDP-forming)
This protein catalyses the successive addition of two glutamate residues to cofactor F420 by two distinct and independent reactions. In the first reaction (EC 6.3.2.31, coenzyme F420-0---L-glutamate ligase) the enzyme attaches a glutamate via its alpha-amine group to F420-0. In the second reaction, which is described here, the enzyme catalyses the addition of a second L-glutamate residue to the gamma-carboxyl of the first glutamate.
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
L-glutamate + dGTP + coenzyme F420-0
dGDP + phosphate + coenzyme F420-1
show the reaction diagram
maximum activity for coenzyme F420-2 formation is 25% of the maximum activity with GTP. Coenzyme F420-1 is coenzyme F420 with one glutamic acid residue (attached via its alpha-NH2 to F420-0), the second glutamate in bound via a gamma ligation
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-
?
L-glutamate + dGTP + coenzyme gamma-F420-1
dGDP + phosphate + coenzyme gamma-F420-2
show the reaction diagram
maximum activity for coenzyme F420-2 formation is 25% of the maximum activity with GTP. Coenzyme F420-1 is coenzyme F420 with one glutamic acid residue (attached via its alpha-NH2 to F420-0), the second glutamate in bound via a gamma ligation
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-
?
L-glutamate + GTP + coenzyme gamma-F420-1
GDP + phosphate + coenzyme gamma-F420-2
show the reaction diagram
L-glutamate + UTP + coenzyme gamma-F420-1
UDP + phosphate + coenzyme gamma-F420-2
show the reaction diagram
maximum activity for coenzyme F420-2 formation is 66% of the maximum activity with GTP. Coenzyme F420-1 is coenzyme F420 with one glutamic acid residue (attached via its alpha-NH2 to F420-0), the second glutamate in bound via a gamma ligation
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?
additional information
?
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CofE incubated with 10 mM beta-glutamate, D-glutamate, gamma-glutamylglutamate, DL-2-amino-3-phosphonopropionic acid, 2-carboxyethylphosphonic acid, or L-R-aminoadipic acid produces no F420-2 or other F420 analogues. CofE cannot use F420-2 as substrate to add more glutamate residues
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?
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
L-glutamate + GTP + coenzyme gamma-F420-1
GDP + phosphate + coenzyme gamma-F420-2
show the reaction diagram
step in the biosynthesis of coenzyme F420
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-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Co2+
divalent cation requirement, maximum CofE activity is observed with the addition of 10 mM MnCl2. Reactions containing 10 mM either MgCl2 or CoCl2 produce 40% of the F420-2 of that is produced with MnCl2
K+
CofE absolutely requires a monovalent cation for activity, the greatest extent of activation is achieved by K+, with maximum stimulation occurring at 0.2 M KCl, NH4+ stimulates activity to a lesser extent, extent, whereas Na+ and Li+ have no effect on CofE activity. A mixture of Mn2+, Mg2+, and K+ is the most effective
Mg2+
divalent cation requirement, maximum CofE activity is observed with the addition of 10 mM MnCl2. Reactions containing 10 mM either MgCl2 or CoCl2 produce 40% of the F420-2 of that is produced with MnCl2. The combination of 5 mM MgCl2 and 2-5 mM of MnCl2 supports the highest activity
Mn2+
divalent cation requirement, maximum CofE activity is observed with the addition of 10 mM MnCl2. Reactions containing 10 mM either MgCl2 or CoCl2 produce 40% of the F420-2 of that is produced with MnCl2. The combination of 5 mM MgCl2 and 2-5 mM of MnCl2 supports the highest activity
NH4+
CofE absolutely requires a monovalent cation for activity, the greatest extent of activation is achieved by K+, NH4+ stimulates activity to a lesser extent, whereas Na+ and Li+ have no effect on CofE activity. A mixture of Mn2+, Mg2+, and K+ is the most effective
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
beta,gamma-CH2-GTP
5 mM, 56% inhibition
Cs2+
in the presence of either Rb+ or Cs+ at 0.2 M concentration no gamma-F420-2 is formed
GDP
5 mM, 67% inhibition
Ni2+
in the presence of NiCl2 no gamma-F420-2 is formed
Rb+
in the presence of either Rb+ or Cs+ at 0.2 M concentration no gamma-F420-2 is formed
additional information
no significant inhibition when CofE is incubated with the following compound (10 mM): L-aspartate, L-glutamine, L-homocysteic acid, or DL-amino-4-phosphono-butyric acid
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
no change of CofE activity is observed when the enzyme is assayed with the addition of 10 mM dithiothreitol to the reaction mixture
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.00021
coenzyme gamma-F420-1
pH 8.5, 50°C
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
8.5
with 50 mM CHES/Na+ buffer
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
35 - 80
35°C: about 30% of maximal activity, 80°C: about 55% of maximal activity
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
27150
2 * 27150, calculated from sequence
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
homodimer
2 * 27150, calculated from sequence
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
80
15 min, 30% loss of activity
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Li, H.; Graupner, M.; Xu, H.; White, R.H.
CofE catalyzes the addition of two glutamates to F420-0 in F420 coenzyme biosynthesis in Methanococcus jannaschii
Biochemistry
42
9771-9778
2003
Methanocaldococcus jannaschii (Q58178)
Manually annotated by BRENDA team