Information on EC 3.5.1.55 - long-chain-fatty-acyl-glutamate deacylase
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IUBMB CommentsDoes not act on acyl derivates of other amino acids. Optimum chain length of acyl residue is 12 to 16.
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
Synonyms
long-chain acylglutamate amidase, long-chain aminoacylase, long-chain-fatty-acyl-glutamate deacylase, N-acyl-D-glutamate deacylase,
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long-chain acylglutamate amidase
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long-chain aminoacylase
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long-chain-fatty-acyl-glutamate deacylase
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N-acyl-D-glutamate deacylase
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N-long-chain-fatty-acyl-L-glutamate + H2O = a long-chain carboxylate + L-glutamate
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hydrolysis of linear amides
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N-long-chain-fatty-acyl-L-glutamate amidohydrolase
Does not act on acyl derivates of other amino acids. Optimum chain length of acyl residue is 12 to 16.
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N-arachidonoyl-L-glutamate + H2O
arachidonate + L-glutamate
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32% of the activity with N-decanoyl-L-glutamate
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N-benzoyl-L-glutamate + H2O
benzoate + L-glutamate
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74% of the activity with N-decanoyl-L-glutamate
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N-decanoyl-L-glutamate + H2O
decanoate + L-glutamate
N-lauroyl-L-aspartate + H2O
lauroate + L-aspartate
N-lauroyl-L-glutamate + H2O
lauroate + L-glutamate
N-lauroylglycine + H2O
lauroate + glycine
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17.5% of the activity with palmitoyl-L-glutamate
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N-myristoyl-L-glutamate + H2O
myristoate + L-glutamate
N-octanoyl-L-glutamate + H2O
octanoate + L-glutamate
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80% of the activity with decanoyl-L-glutamate
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N-oleoyl-L-glutamate + H2O
oleate + L-glutamate
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67% of the activity with N-decanoyl-L-glutamate
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N-palmitoyl-L-glutamate + H2O
palmitate + L-glutamate
N-pentadecanoyl-L-glutamate + H2O
pentadecanoate + L-glutamate
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best substrate
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N-stearoyl-L-glutamate + H2O
stearate + L-glutamate
N-undecanoyl-L-glutamate + H2O
undecanoate + L-glutamate
additional information
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N-decanoyl-L-glutamate + H2O
decanoate + L-glutamate
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best substrate
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N-decanoyl-L-glutamate + H2O
decanoate + L-glutamate
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best substrate
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N-lauroyl-L-aspartate + H2O
lauroate + L-aspartate
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N-lauroyl-L-aspartate + H2O
lauroate + L-aspartate
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54% of the activity with palmitoyl-L-glutamate
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N-lauroyl-L-glutamate + H2O
lauroate + L-glutamate
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85% of the activity with palmitoyl-L-glutamate
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N-lauroyl-L-glutamate + H2O
lauroate + L-glutamate
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C12, 99% of the activity with pentadecanoyl-L-glutamate
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N-lauroyl-L-glutamate + H2O
lauroate + L-glutamate
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88% of the activity with N-decanoyl-L-glutamate
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N-lauroyl-L-glutamate + H2O
lauroate + L-glutamate
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88% of the activity with N-decanoyl-L-glutamate
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N-myristoyl-L-glutamate + H2O
myristoate + L-glutamate
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91% of the activity with palmitoyl-L-glutamate
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N-myristoyl-L-glutamate + H2O
myristoate + L-glutamate
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51% of the activity with N-decanoyl-L-glutamate
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N-myristoyl-L-glutamate + H2O
myristoate + L-glutamate
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C14, 97% of the activity with pentadecanoyl-L-glutamate
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N-myristoyl-L-glutamate + H2O
myristoate + L-glutamate
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N-myristoyl-L-glutamate + H2O
myristoate + L-glutamate
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N-palmitoyl-L-glutamate + H2O
palmitate + L-glutamate
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best substrate
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N-palmitoyl-L-glutamate + H2O
palmitate + L-glutamate
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C16, 60% of the activity with pentadecanoyl-L-glutamate
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N-palmitoyl-L-glutamate + H2O
palmitate + L-glutamate
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49% of the activity with N-decanoyl-L-glutamate
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N-palmitoyl-L-glutamate + H2O
palmitate + L-glutamate
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49% of the activity with N-decanoyl-L-glutamate
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N-stearoyl-L-glutamate + H2O
stearate + L-glutamate
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28% of the activity with palmitoyl-L-glutamate
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N-stearoyl-L-glutamate + H2O
stearate + L-glutamate
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36% of the activity with pentadecanoyl-L-glutamate
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N-stearoyl-L-glutamate + H2O
stearate + L-glutamate
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67% of the activity with N-decanoyl-L-glutamate
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N-undecanoyl-L-glutamate + H2O
undecanoate + L-glutamate
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51% of the activity with palmitoyl-L-glutamate
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N-undecanoyl-L-glutamate + H2O
undecanoate + L-glutamate
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73% of the activity with pentadecanoyl-L-glutamate
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additional information
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not: acetyl-L-glutamate
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additional information
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enzyme I is almost specific to the lipoamino acids containing L-glutamate
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additional information
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enzyme II shows broader substrate specificity than enzyme I and catalyzes the hydrolysis of lipoamino acids containing various amino acid residues
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additional information
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does not act on acyl derivatives of other amino acids
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additional information
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not: acetyl-L-glutamate
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additional information
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not: acetyl-L-glutamate
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Hg2+
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PCMB
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1.4
N-lauroyl-L-aspartate
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0.17 - 7.1
N-lauroyl-L-glutamate
0.083 - 5
N-myristoyl-L-glutamate
0.21
N-oleolyl-L-glutamate
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0.21
N-oleoyl-L-glutamate
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0.14 - 4.9
N-palmitoyl-L-glutamate
0.33 - 2
N-stearoyl-L-glutamate
0.17
N-lauroyl-L-glutamate
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7.1
N-lauroyl-L-glutamate
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0.083
N-myristoyl-L-glutamate
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5
N-myristoyl-L-glutamate
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0.14
N-palmitoyl-L-glutamate
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4.9
N-palmitoyl-L-glutamate
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0.33
N-stearoyl-L-glutamate
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2
N-stearoyl-L-glutamate
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6 - 9
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substrate lauroyl-DL-valine, lauroylglycine
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substrate N-tearoyl-L-glutamate
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substrate N-lauroyl-L-glutamate, N-myristoyl-L-glutamate
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N-lauroyl-L-aspartate, N-lauroyl-L-phenylalanine, N-palmitoyl-L-glutamate; substrate N-lauroyl-L-glutamate, N-myristoyl-L-glutamate
8.5
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substrate N-palmitoyl-L-glutamate
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brenda
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brenda
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brenda
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brenda
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brenda
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220000
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enzyme II, gel filtration
300000
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enzyme I, gel filtration
40000
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8 * 40000, enzyme I, SDS -PAGE
55000
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4 * 55000, enzyme II, SDS-PAGE
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octamer
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8 * 40000, enzyme I, SDS -PAGE
tetramer
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4 * 55000, enzyme II, SDS-PAGE
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4 - 11
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4°C, 24 h, stable, enzyme form II
209198
6
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4°C, 24 h, 60% loss of activity, enzyme form I
209197
6 - 8
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30°C, 5 h, stable
209199
7 - 11
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4°C, 24 h, stable, enzyme form I
209197
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55
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pH 7, 10 min, almost complete loss of activity, enzyme II
60
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pH 7, 10 min, quite stable, enzyme form I
70
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pH 7, 10 min, complete inactivation, enzyme form I
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pH 7.0, 10 min, 50% loss of activity, enzyme II
40
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pH 8.0, 15 min, stable
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Fukuda, H.; Iwade, S.; Kimura, A.
A new enzyme: long acyl aminoacylase from Pseudomonas diminuta
J. Biochem.
91
1731-1738
1982
Brevundimonas diminuta
brenda
Shintani, Y.; Fukuda, H.; Okamoto, N.; Murata, K.; Kimura, A.
Isolation and characterization of N-long chain acyl aminoacylase from Pseudomonas diminuta
J. Biochem.
96
637-643
1984
Brevundimonas diminuta
brenda
Murase, H.; Kunieda, T.; Terao, J.; Nagao, A.
Purification and characterisation of long chain acyl aminoacylase from Penicillium sp. B-001
Biosci. Biotechnol. Biochem.
57
854-855
1993
Penicillium sp., Penicillium sp. B-001
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brenda
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3.5.1.55 long-chain-fatty-acyl-glutamate deacylase
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