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 ACCESSION NO.
LITERATURE
GTP + coenzyme F420-0 + L-glutamate = GDP + phosphate + coenzyme F420-1
show the reaction diagram
-
-
-
-
PATHWAY
KEGG Link
MetaCyc Link
factor 420 polyglutamylation
-
Methane metabolism
-
Microbial metabolism in diverse environments
-
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.
SYNONYMS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
F420-0:gamma-glutamyl ligase
Q58178
-
ORGANISM
COMMENTARY
LITERATURE
SEQUENCE CODE
SEQUENCE DB
SOURCE
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
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
-
-
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
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 ACCESSION NO.
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 ACCESSION NO.
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
-
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
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT ACCESSION NO.
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
-
KM VALUE [mM]
KM VALUE [mM] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.001
-
coenzyme gamma-F420-0
-, Q58178
pH 8.5, 50C
-
pH OPTIMUM
pH MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
8.5
-
-, Q58178
with 50 mM CHES/Na+ buffer
8.5
-
O28028
assay at
TEMPERATURE OPTIMUM
TEMPERATURE OPTIMUM MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
TEMPERATURE RANGE
TEMPERATURE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
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
MOLECULAR WEIGHT MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
52100
-
-, Q58178
gel filtration
SUBUNITS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
homodimer
-, Q58178
2 * 27150, calculated from sequence
Crystallization/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
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
TEMPERATURE STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
80
-
-, Q58178
15 min, 30% loss of activity
Purification/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
recombinant enzyme
-, Q58178
Cloned/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
expressed in Escherichia coli
-, Q58178