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Ligand allylglycine Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Basic Ligand Information Molecular Structure
C5 H9 NO2
allylglycine
WNNNWFKQCKFSDK-BYPYZUCNSA-N
L-2-amino-4-pentenoate, L-allyl-Gly, L-Allylglycine
Roles as Enzyme Ligand
In Vivo Substrate in Enzyme-catalyzed Reactions (1 result)Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
ATP + allylglycine + tRNALeu = AMP + diphosphate + allylglycyl-tRNALeu
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Substrate in Enzyme-catalyzed Reactions (3 results)
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L-2-amino-4-pentenoate + H2O + NAD+ = 2-oxo-4-pentenoate + NH3 + NADH
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ATP + allylglycine + tRNALeu = AMP + diphosphate + allylglycyl-tRNALeu
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L-2-aminoadipate + allylglycine + L-valine + ATP = L-delta-(aminoadipyl)-L-allylglycinyl-D-valine + AMP + diphosphate
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Product in Enzyme-catalyzed Reactions (1 result)
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L-allyl-Gly-7-amido-4-carbamoylmethylcoumarin + H2O = L-allyl-Gly + 7-amino-4-carbamoylmethylcoumarin
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Inhibitor in Enzyme-catalyzed Reactions (3 results)
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irreversible inactivation
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3D Structure of Enzyme-Ligand-Complex (PDB) (1 result)
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Enzyme Kinetic Parameters
Ki Value (1 result)
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References & Links Literature References (7)
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Over-production, purification and properties of the uridine-diphosphate-N-acetylmuramate:L-alanine ligase from Escherichia coli
1995
Liger, S.; Masson, A.; Blanot, D.; van Heijenoort, J.; Parquet, C.
Eur. J. Biochem.
230
80-87
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Substrate specificity of L-delta-(alpha-aminoadipoyl)-L-cysteinyl-D-valine synthetase from Cephalosporium acremonium: demonstration of the structure of several unnatural tripeptide products
1994
Baldwin, J.E.; Shiau, C.Y.; Byford, M.F.; Schofield, C.J.
Biochem. J.
301
367-372
Mechanism for the desulfurization of L-cysteine catalyzed by the nifS gene product
1994
Zheng, L.; White, R.H.; Cash, V.L.; Dean, D.R.
Biochemistry
33
4714-4720
Attenuation of the editing activity of the Escherichia coli leucyl-tRNA synthetase allows incorporation of novel amino acids into proteins in vivo
2002
Tang, Y.; Tirrell, D.A.
Biochemistry
41
10635-10645
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An improved method for production of recombinant human glutamic acid decarboxylase 65 for use in phytopharmaceutical assessment
2008
Awad, R.; Crump, K.; Mullally, M.; Sardana, R.K.; Arnason, J.T.; Trudeau, V.L.
Pharm. Biol.
46
72-81
Alteration of substrate specificity of alanine dehydrogenase
2015
Fernandes, P.; Aldeborgh, H.; Carlucci, L.; Walsh, L.; Wasserman, J.; Zhou, E.; Lefurgy, S.; Mundorff, E.
Protein Eng. Des. Sel.
28
29-35
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An improved method for production of recombinant human glutamic acid decarboxylase 65 for use in phytopharmaceutical assessment
2008
Awad, R.; Crump, K.; Mullally, M.; Sardana, R.K.; Arnason, J.T.; Trudeau, V.L.
Pharm. Biol.
46
72-81
Links to other databases for allylglycine
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