Information on EC 6.3.2.B16 - L-valine-specific L-amino acid ligase

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The expected taxonomic range for this enzyme is: Bacillus subtilis

EC NUMBER
COMMENTARY hide
6.3.2.B16
preliminary BRENDA-supplied EC number
RECOMMENDED NAME
GeneOntology No.
L-valine-specific L-amino acid ligase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
2 ATP + L-valine + 2 L-Baa = 2 ADP + 2 phosphate + L-Val-(L-Baa)2
show the reaction diagram
3 ATP + 3 L-valine + L-Zaa = 3 ADP + 3 phosphate + L-Val-L-Val-L-Val-L-amino-acid-L-Zaa
show the reaction diagram
ATP + 2 L-valine + L-Yaa = 2 ADP + 2 phosphate + L-Val-L-Val-L-Yaa
show the reaction diagram
n-1 ATP + n L-Xaa = n-1 ADP + n-1 phosphate + (Xaa)n
show the reaction diagram
SYSTEMATIC NAME
IUBMB Comments
L-valine:L-amino acid ligase (ADP-forming, oligopeptide-forming)
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
metabolism
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
2 ATP + 2 L-Val + Gly
2 ADP + 2 phosphate + L-Val-L-Val-Gly
show the reaction diagram
-
-
-
?
2 ATP + 2 L-Val + L-Ala
2 ADP + 2 phosphate + L-Val-L-Val-L-Ala
show the reaction diagram
2 ATP + 2 L-Val + L-Arg
2 ADP + 2 phosphate + L-Val-L-Val-L-Arg
show the reaction diagram
2 ATP + 2 L-Val + L-Asn
2 ADP + 2 phosphate + L-Val-L-Val-L-Asn
show the reaction diagram
-
-
-
?
2 ATP + 2 L-Val + L-Gln
2 ADP + 2 phosphate + L-Val-L-Val-L-Gln
show the reaction diagram
-
-
-
?
2 ATP + 2 L-Val + L-His
2 ADP + 2 phosphate + L-Val-L-Val-L-His
show the reaction diagram
-
-
-
?
2 ATP + 2 L-Val + L-Ile
2 ADP + 2 phosphate + L-Val-L-Val-L-Ile
show the reaction diagram
-
-
-
?
2 ATP + 2 L-Val + L-Leu
2 ADP + 2 phosphate + L-Val-L-Val-L-Leu
show the reaction diagram
-
-
-
?
2 ATP + 2 L-Val + L-Lys
2 ADP + 2 phosphate + L-Val-L-Val-L-Lys
show the reaction diagram
-
-
-
?
2 ATP + 2 L-Val + L-Met
2 ADP + 2 phosphate + L-Val-L-Val-L-Met
show the reaction diagram
-
-
-
?
2 ATP + 2 L-Val + L-Phe
2 ADP + 2 phosphate + L-Val-L-Val-L-Phe
show the reaction diagram
-
-
-
?
2 ATP + 2 L-Val + L-Ser
2 ADP + 2 phosphate + L-Val-L-Val-L-Ser
show the reaction diagram
-
-
-
?
2 ATP + 2 L-Val + L-Thr
2 ADP + 2 phosphate + L-Val-L-Val-L-Thr
show the reaction diagram
-
-
-
?
2 ATP + 2 L-Val + L-Trp
2 ADP + 2 phosphate + L-Val-L-Val-L-Trp
show the reaction diagram
-
-
-
?
2 ATP + 3 L-leucine
2 ADP + 2 phosphate + L-Leu-L-Leu-L-Leu
show the reaction diagram
the enzyme synthesizes homo-oligomers of two to five amino acids. ATP cannot by replaced with GTP, CTP or dTTP
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-
?
2 ATP + 3 L-methionine
2 ADP + 2 phosphate + L-Met-L-Met-L-Met
show the reaction diagram
the enzyme synthesizes homo-oligomers of two to five amino acids. ATP cannot by replaced with GTP, CTP or dTTP
-
-
?
2 ATP + 3 L-valine
2 ADP + 2 phosphate + L-Val-L-Val-L-Val
show the reaction diagram
2 ATP + L-Val + 2 L-Leu
2 ADP + 2 phosphate + L-Val-L-Leu-L-Leu
show the reaction diagram
-
-
-
?
2 ATP + L-Val + 2 L-Met
2 ADP + 2 phosphate + L-Met-L-Met-L-Met
show the reaction diagram
-
-
-
?
2 ATP + L-Val + L-Arg-L-Ser
2 ADP + phosphate + L-Val-L-Arg-L-Ser
show the reaction diagram
no homopeptides of Val-Val and Val-Val-Val are detected. This suggests that the enzyme preferentially uses dipeptides as the C-terminal substrate
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-
?
2 ATP + L-Val + L-Val + L-Arg-L-Ser
2 ADP + 2 phosphate + L-Val-L-Val-L-Arg-L-Ser
show the reaction diagram
no homopeptides of Val-Val and Val-Val-Val are detected. This suggests that the enzyme preferentially uses dipeptides as the C-terminal substrate
-
-
?
2 ATP + Val + 2 L-Ile
2 ADP + 2 phosphate + L-Val-L-Ile-L-Ile
show the reaction diagram
-
-
-
?
3 ATP + 3 L-Val + L-Arg
3 ADP + 3 phosphate + L-Val-L-Val-L-Val-L-Arg
show the reaction diagram
-
-
-
?
3 ATP + 3 L-Val + L-Gln
3 ADP + 3 phosphate + L-Val-L-Val-L-Asn
show the reaction diagram
-
-
-
?
3 ATP + 3 L-Val + L-Gln
3 ADP + 3 phosphate + L-Val-L-Val-L-Gln
show the reaction diagram
-
-
-
?
3 ATP + 3 L-Val + L-His
3 ADP + 3 phosphate + L-Val-L-Val-L-Val-L-His
show the reaction diagram
-
-
-
?
3 ATP + 3 L-Val + L-Phe
3 ADP + 3 phosphate + L-Val-L-Val-L-Val-L-Phe
show the reaction diagram
-
-
-
?
3 ATP + 4 L-leucine
3 ADP + 3 phosphate + L-Leu-L-Leu-L-Leu-L-Leu
show the reaction diagram
the enzyme synthesizes homo-oligomers of two to five amino acids. ATP cannot by replaced with GTP, CTP or dTTP
-
-
?
3 ATP + 4 L-methionine
3 ADP + 3 phosphate + L-Met-L-Met-L-Met-L-Met
show the reaction diagram
the enzyme synthesizes homo-oligomers of two to five amino acids. ATP cannot by replaced with GTP, CTP or dTTP
-
-
?
3 ATP + 4 L-valine
3 ADP + 3 phosphate + L-Val-L-Val-L-Val-L-Val
show the reaction diagram
4 ATP + 5 L-leucine
4 ADP + 4 phosphate + L-Leu-L-Leu-L-Leu-L-Leu-L-Leu
show the reaction diagram
the enzyme synthesizes homo-oligomers of two to five amino acids. ATP cannot by replaced with GTP, CTP or dTTP
-
-
?
4 ATP + 5 L-methionine
4 ADP + 4 phosphate + L-Met-L-Met-L-Met-L-Met-L-Met
show the reaction diagram
the enzyme synthesizes homo-oligomers of two to five amino acids. ATP cannot by replaced with GTP, CTP or dTTP
-
-
?
4 ATP + 5 L-valine
4 ADP + 4 phosphate + L-Val-L-Val-L-Val-L-Val-L-Val
show the reaction diagram
the enzyme synthesizes homo-oligomers of two to five amino acids. ATP cannot by replaced with GTP, CTP or dTTP
-
-
?
ATP + 2 L-leucine
ADP + phosphate + L-Leu-L-Leu
show the reaction diagram
the enzyme synthesizes homo-oligomers of two to five amino acids. ATP cannot by replaced with GTP, CTP or dTTP
-
-
?
ATP + 2 L-methionine
ADP + phosphate + L-Met-L-Met
show the reaction diagram
the enzyme synthesizes homo-oligomers of two to five amino acids. ATP cannot by replaced with GTP, CTP or dTTP
-
-
?
ATP + 2 L-valine
ADP + phosphate + L-Val-L-Val
show the reaction diagram
ATP + L-Val + L-Arg
ADP + phosphate + L-Val-L-Arg
show the reaction diagram
-
-
-
?
ATP + L-Val + L-Arg-L-Ser
ADP + phosphate + L-Val-L-Arg-L-Ser + L-Val-L-Val-L-Arg-L-Ser
show the reaction diagram
no homopeptides of Val-Val and Val-Val-Val are detected. The enzyme preferentially uses dipeptides as the C-terminal substrates
-
-
?
ATP + L-Val + L-Arg-NHOH
ADP + phosphate + L-Val-L-Arg-NHOH + L-Val-L-Val-L-Arg-NHOH
show the reaction diagram
-
-
-
?
ATP + L-Val + L-Phe-NHOH
ADP + phosphate + L-Val-L-Phe-NHOH + L-Val-L-Val-L-Phe-NHOH
show the reaction diagram
-
-
-
?
ATP + L-valine + L-Val-L-Val
ADP + phosphate + L-Val-L-Val-L-Val
show the reaction diagram
ATP + L-valine + L-Val-L-Val-L-Val
ADP + phosphate + L-Val-L-Val-L-Val-L-Val
show the reaction diagram
additional information
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
ATP
dependent on, cannot be replaced by GTP, CTP, or TTP
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Co2+
can replace Mg2+, but with lower activity; required. Mg2+ can be replaced with Mn2+ and Co2+. The use of Mn2+ or Co2+ decreases activity and the maximum length of peptide synthesized becomes shorter
Mg2+
required, best metal cofactor, can be replaced by Mn2+ or Co2+; required. Mg2+ can be replaced with Mn2+ and Co2+. The use of Mn2+ or Co2+ decreases activity and the maximum length of peptide synthesized becomes shorter
Mn2+
can replace Mg2+, but with lower activity; required. Mg2+ can be replaced with Mn2+ and Co2+. The use of Mn2+ or Co2+ decreases activity and the maximum length of peptide synthesized becomes shorter
additional information
in the reaction with Val, tetramers are the longest products synthesized, trimer are formed with Co2+
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
9
about, recombinant enzyme
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.5 - 9.5
activity range, recombinant enzyme, profile overview
8 - 10
pH 8.0: about 50% of maximal activity, significant decrease in activity above pH 10.0
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
40
; recombinant enzyme
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
25 - 45
activity range, recombinant enzyme, profile overview
30 - 45
30°C: about 35% of maximal activity, 45°C: about 80% of maximal activity
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
; recombinant His-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography and gel filtration
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli as His-tagged protein; gene rizB, two splicing variants, rizB-P1 and rizB-P2, transcriptional analysis and DNA and amino acid sequence determination and analysis, sequence comparison, recombinant overexpression of the His-tagged enzyme in Escherichia coli strain BL21(DE3)