Information on EC 6.3.2.34 - coenzyme F420-1:gamma-L-glutamate ligase

Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Specify your search results
Select one or more organisms in this record:
Show additional data
Do not include text mining results
Include (text mining) results (more...)
Include results (AMENDA + additional results, but less precise; more...)

The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
6.3.2.34
-
RECOMMENDED NAME
GeneOntology No.
coenzyme F420-1:gamma-L-glutamate ligase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
GTP + coenzyme F420-1 + L-glutamate = GDP + phosphate + coenzyme gamma-F420-2
show the reaction diagram
-
-
-
-
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
factor 420 polyglutamylation
-
-
Methane metabolism
-
-
Microbial metabolism in diverse environments
-
-
factor 420 biosynthesis
-
-
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.
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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
UDP + phosphate + coenzyme gamma-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
-
-
?
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
-
-
?
L-glutamate + GTP + coenzyme F420-1
GDP + phosphate + coenzyme gamma-F420-2
show the reaction diagram
the enzyme protein catalyzes two distinct and independent reactions, firstly attaching a glutamte via its alpha-NH2 to F420-0 (cf. coenzyme F420-0:glutamyl ligase). The second reaction is a gamma ligation, taking place when a certain amount of monoglutamylated F420-1 has accumulated
-
-
?
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
-
-
?
additional information
?
-
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
-
-
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
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 F420-1
GDP + phosphate + coenzyme gamma-F420-2
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 (cf. coenzyme F420-0:glutamyl ligase). The second reaction is a gamma ligation, taking place when a certain amount of monoglutamylated F420-1 has accumulated
-
-
?
L-glutamate + GTP + coenzyme gamma-F420-1
GDP + phosphate + coenzyme gamma-F420-2
show the reaction diagram
Q58178
step in the biosynthesis of coenzyme F420
-
-
?
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
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
INHIBITORS
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
Rb2+
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
-
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
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.00021
coenzyme gamma-F420-1
pH 8.5, 50C
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
35 - 80
35C: about 30% of maximal activity, 80C: about 55% of maximal activity
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
27150
2 * 27150, calculated from sequence
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
homodimer
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
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
Show AA Sequence (814 entries)
Please use the Sequence Search for a specific query.