Information on EC 6.3.2.31 - coenzyme F420-0:L-glutamate ligase

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The expected taxonomic range for this enzyme is: Euryarchaeota

EC NUMBER
COMMENTARY
6.3.2.31
-
RECOMMENDED NAME
GeneOntology No.
coenzyme F420-0:L-glutamate ligase
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
GTP + coenzyme F420-0 + L-glutamate = GDP + phosphate + coenzyme F420-1
show the reaction diagram
-
-
-
-
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
factor 420 biosynthesis
-
-
factor 420 polyglutamylation
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-
Methane metabolism
-
-
Microbial metabolism in diverse environments
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-
SYSTEMATIC NAME
IUBMB Comments
L-glutamate:coenzyme F420-0 ligase (GDP-forming)
This protein catalyses the successive addition of two glutamate residues to cofactor F420 by two distinct and independent reactions. In the reaction described here the enzyme attaches a glutamate via its alpha-amine group to F420-0. In the second reaction (EC 6.3.2.34, coenzyme F420-1---gamma-L-glutamate ligase) it catalyses the addition of a second L-glutamate residue to the gamma-carboxyl of the first glutamate.
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
L-glutamate + ATP + coenzyme F420-0
ADP + phosphate + coenzyme F420-1
show the reaction diagram
Q58178
-
-
-
?
L-glutamate + dGTP + coenzyme F420-0
UDP + phosphate + coenzyme F420-1
show the reaction diagram
Q58178
coenzyme F420-1 is coenzyme F420 with one glutamic acid residue attached via its alpha-NH2 to F420-0
-
-
?
L-glutamate + GTP + coenzyme F420-0
GDP + phosphate + coenzyme gamma-F420-1
show the reaction diagram
Q58178
step in the biosynthesis of coenzyme F420
-
-
?
L-glutamate + GTP + coenzyme F420-0
GDP + phosphate + coenzyme gamma-F420-1
show the reaction diagram
O28028
the enzyme protein catalyzes two distinct and independent reactions, firstly attaching a glutamte via its alpha-NH2 to F420-0. The second reaction (cf. coenzyme F420-1:gamma-glutamyl ligase) is a gamma ligation, taking place when a certain amount of monoglutamylated F420-1 has accumulated
-
-
?
L-glutamate + GTP + coenzyme F420-0
GDP + phosphate + coenzyme F420-1
show the reaction diagram
Q58178
coenzyme F420-1 is coenzyme F420 with one glutamic acid residue attached via its alpha-NH2 to F420-0
-
-
?
L-glutamate + UTP + coenzyme F420-0
UDP + phosphate + coenzyme F420-1
show the reaction diagram
Q58178
coenzyme F420-1 is coenzyme F420 with one glutamic acid residue attached via its alpha-NH2 to F420-0
-
-
?
additional information
?
-
Q58178
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 F420-1
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-
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NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
L-glutamate + GTP + coenzyme F420-0
GDP + phosphate + coenzyme gamma-F420-1
show the reaction diagram
Q58178
step in the biosynthesis of coenzyme F420
-
-
?
L-glutamate + GTP + coenzyme F420-0
GDP + phosphate + coenzyme gamma-F420-1
show the reaction diagram
O28028
the enzyme protein catalyzes two distinct and independent reactions, firstly attaching a glutamte via its alpha-NH2 to F420-0. The second reaction (cf. coenzyme F420-1:gamma-glutamyl ligase) is a gamma ligation, taking place when a certain amount of monoglutamylated F420-1 has accumulated
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Co2+
Q58178
divalent cation requirement, maximum CofE activity is observed with the addition of 10 mM MnCl2
K+
Q58178
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+
Q58178
divalent cation requirement, maximum CofE activity is observed with the addition of 10 mM MnCl2. The combination of 5 mM MgCl2 and 2-5 mM of MnCl2 supports the highest activity
Mn2+
Q58178
divalent cation requirement, maximum CofE activity is observed with the addition of 10 mM MnCl2. The combination of 5 mM MgCl2 and 2-5 mM of MnCl2 supports the highest activity
Mn2+
O28028
there are two Mn2+-binding sites per monomer within close proximity of the GDP alpha and beta-phosphate groups
NH4+
Q58178
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
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
beta,gamma-CH2-GTP
Q58178
5 mM, 56% inhibition
Ca2+
Q58178
10 mM, only 26% F420-0 is converted to F420-1
Cs2+
Q58178
in the presence of either Rb+ or Cs+ at 0.2 M concentration, the only product of reaction is F420-1
Rb2+
Q58178
in the presence of either Rb+ or Cs+ at 0.2 M concentration, the only product of reaction is F420-1
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Zn2+
Q58178
10 mM, only 26% F420-0 is converted to F420-1
GDP
Q58178
5 mM, 67% inhibition
additional information
Q58178
no significant inhibition when CofE is incubated with the following compound (10 mM): L-aspartate, Lglutamine, L-homocysteic acid, or DL-amino-4-phosphono-butyric acid
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
Q58178
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
LITERATURE
IMAGE
0.001
coenzyme gamma-F420-0
Q58178
pH 8.5, 50C
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
8.5
Q58178
with 50 mM CHES/Na+ buffer
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
35 - 80
Q58178
35C: about 30% of maximal activity, 80C: about 55% of maximal activity
PDB
SCOP
CATH
ORGANISM
Archaeoglobus fulgidus (strain ATCC 49558 / VC-16 / DSM 4304 / JCM 9628 / NBRC 100126)
Archaeoglobus fulgidus (strain ATCC 49558 / VC-16 / DSM 4304 / JCM 9628 / NBRC 100126)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
52100
Q58178
gel filtration
696202
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
homodimer
Q58178
2 * 27150, calculated from sequence
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
crystal structure of the enzyme from Archaeoglobus fulgidus and its complex with GDP at 2.5 A and 1.35 A resolution, respectively. CofE-AF crystallization is performed by the sitting-drop and hanging-drop methods using vapor diffusion at 18C
O28028
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
80
Q58178
15 min, 30% loss of activity
696202
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
recombinant enzyme
Q58178
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli
Q58178