Information on EC 6.3.4.24 - tyramine-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 expected taxonomic range for this enzyme is: Methanocaldococcus fervens

EC NUMBER
COMMENTARY hide
6.3.4.24
-
RECOMMENDED NAME
GeneOntology No.
tyramine-L-glutamate ligase
-
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
ATP + tyramine + L-glutamate = ADP + phosphate + gamma-glutamyltyramine
show the reaction diagram
-
-
-
-
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Methane metabolism
-
-
methanofuran biosynthesis
SYSTEMATIC NAME
IUBMB Comments
tyramine:L-glutamate gamma-ligase (ADP-forming)
The enzyme, which has been characterized from the archaea Methanocaldococcus fervens, participates in the biosynthesis of the cofactor methanofuran. Requires a divalent cation for activity, with Mn2+ giving the highest activity, followed by Mg2+, Co2+, Zn2+, and Fe2+.
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
ATP + tyramine + L-glutamate
ADP + phosphate + gamma-glutamyltyramine
show the reaction diagram
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
ATP + tyramine + L-glutamate
ADP + phosphate + gamma-glutamyltyramine
show the reaction diagram
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Co2+
the enzyme requires a divalent cation for activity. Maximum activity (100%) is observed with the addition of 10 mM Mn2+, followed by 89%, 56%, 46%, and 46% of relative activity by addition of 10 mM Mg2+, Co2+, Zn2+, and Fe2+, respectively. Less than 5% relative activities are observed when 10 mM Ni2+ or Ca2+ is added. However, no activity is detected by addition of Cu2+ or K+
Fe2+
the enzyme requires a divalent cation for activity. Maximum activity (100%) is observed with the addition of 10 mM Mn2+, followed by 89%, 56%, 46%, and 46% of relative activity by addition of 10 mM Mg2+, Co2+, Zn2+, and Fe2+, respectively. Less than 5% relative activities are observed when 10 mM Ni2+ or Ca2+ is added. However, no activity is detected by addition of Cu2+ or K+
Mg2+
the enzyme requires a divalent cation for activity. Maximum activity (100%) is observed with the addition of 10 mM Mn2+, followed by 89%, 56%, 46%, and 46% of relative activity by addition of 10 mM Mg2+, Co2+, Zn2+, and Fe2+, respectively. Less than 5% relative activities are observed when 10 mM Ni2+ or Ca2+ is added. However, no activity is detected by addition of Cu2+ or K+
Mn2+
the enzyme requires a divalent cation for activity. Maximum activity (100%) is observed with the addition of 10 mM Mn2+, followed by 89%, 56%, 46%, and 46% of relative activity by addition of 10 mM Mg2+, Co2+, Zn2+, and Fe2+, respectively. Less than 5% relative activities are observed when 10 mM Ni2+ or Ca2+ is added. However, no activity is detected by addition of Cu2+ or K+
Zn2+
the enzyme requires a divalent cation for activity. Maximum activity (100%) is observed with the addition of 10 mM Mn2+, followed by 89%, 56%, 46%, and 46% of relative activity by addition of 10 mM Mg2+, Co2+, Zn2+, and Fe2+, respectively. Less than 5% relative activities are observed when 10 mM Ni2+ or Ca2+ is added. However, no activity is detected by addition of Cu2+ or K+
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1.5 - 3
ATP
2.3 - 7.3
L-glutamate
0.6 - 1.1
tyramine
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.07 - 5.9
ATP
1.3 - 5.8
L-glutamate
0.05 - 4.8
tyramine
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.02 - 3.9
ATP
4
0.36 - 2.5
L-glutamate
41
0.06 - 6
tyramine
280
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.7
broad pH optimum with a maximum around pH 6.7
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.3 - 10.5
pH 6.3: about 80% of maximal activity, pH 10.5: about 60% of maximal activity
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
33000
x * 33000, SDS-PAGE
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
80
wild-type MfnD and its three variants (E21Q, R251A and T253V). No protein aggregation and precipitation is observed when proteins are incubated for 10 min at 80 °C in 25 mM Tricine/CAPS/TES buffer at pH 10.5
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
E21Q
mutation causes a 3fold decrease in kcat(app) and a slight increase in KM(glutamate). The apparent second-order constants kcat/KM is comparable to the wild type
R251A
mutation causes a 100fold decrease in kcat(app) and a more than 20fold increase in KM(glutamate), indicating that it plays an important role in catalysis
T253V
mutation causes a 3fold decrease in kcat(app). The apparent second-order constants kcat/KM is comparable to the wild type
E21Q
-
mutation causes a 3fold decrease in kcat(app) and a slight increase in KM(glutamate). The apparent second-order constants kcat/KM is comparable to the wild type
-
R251A
-
mutation causes a 100fold decrease in kcat(app) and a more than 20fold increase in KM(glutamate), indicating that it plays an important role in catalysis
-
T253V
-
mutation causes a 3fold decrease in kcat(app). The apparent second-order constants kcat/KM is comparable to the wild type
-