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 hide
6.3.2.31
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RECOMMENDED NAME
GeneOntology No.
coenzyme F420-0:L-glutamate ligase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
GTP + coenzyme F420-0 + L-glutamate = GDP + phosphate + coenzyme F420-1
show the reaction diagram
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
factor 420 biosynthesis
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factor 420 polyglutamylation
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Methane metabolism
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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 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 + ATP + coenzyme F420-0
ADP + phosphate + coenzyme F420-1
show the reaction diagram
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?
L-glutamate + dGTP + coenzyme F420-0
UDP + phosphate + coenzyme F420-1
show the reaction diagram
coenzyme F420-1 is coenzyme F420 with one glutamic acid residue attached via its alpha-NH2 to F420-0
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?
L-glutamate + GTP + coenzyme F420-0
GDP + phosphate + coenzyme F420-1
show the reaction diagram
coenzyme F420-1 is coenzyme F420 with one glutamic acid residue attached via its alpha-NH2 to F420-0
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?
L-glutamate + GTP + coenzyme F420-0
GDP + phosphate + coenzyme gamma-F420-1
show the reaction diagram
L-glutamate + UTP + coenzyme F420-0
UDP + phosphate + coenzyme F420-1
show the reaction diagram
coenzyme F420-1 is coenzyme F420 with one glutamic acid residue attached via its alpha-NH2 to F420-0
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?
additional information
?
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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 F420-0
GDP + phosphate + coenzyme gamma-F420-1
show the reaction diagram
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Co2+
divalent cation requirement, maximum CofE activity is observed with the addition of 10 mM 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. 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
Ca2+
10 mM, only 26% F420-0 is converted to F420-1
Cs2+
in the presence of either Rb+ or Cs+ at 0.2 M concentration, the only product of reaction is F420-1
GDP
5 mM, 67% inhibition
Rb2+
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+
10 mM, only 26% F420-0 is converted to F420-1
additional information
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.001
coenzyme gamma-F420-0
pH 8.5, 50C
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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
PDB
SCOP
CATH
ORGANISM
UNIPROT
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)
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
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