Information on EC 4.3.2.5 - peptidylamidoglycolate lyase

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The expected taxonomic range for this enzyme is: Coelomata

EC NUMBER
COMMENTARY hide
4.3.2.5
-
RECOMMENDED NAME
GeneOntology No.
peptidylamidoglycolate lyase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
peptidylamidoglycolate = peptidyl amide + glyoxylate
show the reaction diagram
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-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
amidine-lyase reaction
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-
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SYSTEMATIC NAME
IUBMB Comments
peptidylamidoglycolate peptidyl-amide-lyase (glyoxylate-forming)
The enzyme acts on the product of the reaction catalysed by EC 1.14.17.3 peptidylglycine monooxygenase, thus removing a terminal glycine residue and leaving a des-glycine peptide amide.
CAS REGISTRY NUMBER
COMMENTARY hide
131689-50-4
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
-
-
Manually annotated by BRENDA team
Mus musculus C57BL/6J
-
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
(R)-2-phenylbutyl-alpha-hydroxy-Gly
(R)-2-phenylbutyl-NH2 + glyoxylate
show the reaction diagram
-
-
-
-
?
(R)-O-acetyl-mandelyl-alpha-hydroxyglycine
(R)-O-acetyl-mandelyl-NH2 + glyoxylate
show the reaction diagram
-
-
-
-
?
(S)-2-phenylbutyl-alpha-hydroxy-Gly
(S)-2-phenylbutyl-NH2 + glyoxylate
show the reaction diagram
-
-
-
-
?
(S)-O-acetyl-mandelyl-alpha-hydroxyglycine
(S)-O-acetyl-mandelyl-NH2 + glyoxylate
show the reaction diagram
-
-
-
-
?
acetyl-D-Phe-alpha-hydroxyglycine
acetyl-D-Phe-NH2 + glyoxylate
show the reaction diagram
-
-
-
-
?
acetyl-L-Phe-alpha-hydroxyglycine
acetyl-L-Phe-NH2 + glyoxylate
show the reaction diagram
-
-
-
-
?
alpha-hydroxybenzoylglycine
benzamide + glyoxylate
show the reaction diagram
-
-
-
-
?
alpha-hydroxyglycine-extended peptide
peptidyl amide + glyoxylate
show the reaction diagram
alpha-N-acetyl-Tyr-Val-alpha-hydroxyglycine
alpha-N-acetyl-Tyr-Val-NH2 + glyoxylate
show the reaction diagram
dansyl-Tyr-Val-alpha-hydroxyglycine
dansyl-Tyr-Val-NH2 + glyoxylate
show the reaction diagram
-
-
-
?
N-2,4,6-trinitrophenyl-D-Tyr-L-Val-(S)-alpha-hydroxy-Gly
N-2,4,6-trinitrophenyl-D-Tyr-L-Val-amide + glyoxylate
show the reaction diagram
-
-
-
?
N-benzoyl-alpha-hydroxy-Gly
benzamide + glyoxylate
show the reaction diagram
-
-
-
-
?
Nalpha-acetyl-Tyr-Val-alpha-hydroxyglycine
Nalpha-acetyl-Tyr-Val-NH2 + glyoxylate
show the reaction diagram
peptidylamidoglycolate
peptidyl amide + glyoxylate
show the reaction diagram
trinitrophenyl-D-Tyr-L-Val-alpha-hydroxy-Gly
trinitrophenyl-D-Tyr-L-Val-NH2 + glyoxylate
show the reaction diagram
trinitrophenyl-D-Tyr-Val-alpha-hydroxy-Gly
trinitrophenyl-D-Tyr-Val-NH2 + glyoxylate
show the reaction diagram
-
-
-
?
additional information
?
-
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
N-2,4,6-trinitrophenyl-D-Tyr-L-Val-(S)-alpha-hydroxy-Gly
N-2,4,6-trinitrophenyl-D-Tyr-L-Val-amide + glyoxylate
show the reaction diagram
P19021
-
-
-
?
peptidylamidoglycolate
peptidyl amide + glyoxylate
show the reaction diagram
additional information
?
-
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Cu2+
activates
Mn2+
activates, wild-type
Ni2+
activates
additional information
the reaction is greatly accelerated by addition of such divalent metals as Mn2+, Co2+, Ni2+, Cu2+, Zn2+, and Cd2+, and the restoration of PAL activity by divalent metals
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
(R)-2-phenylbutyl-alpha-hydroxy-Gly
-
-
(S)-2-phenylbutyl-alpha-hydroxy-Gly
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-
2-mercaptoethanol
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acetylmethionyl pyruvate
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competitive inhibition of PGL domain of full expressed enzyme: AE and monofunctional lyase: PGL
acetylphenylalanyl pyruvate
-
competitive inhibition of PGL domain of full expressed enzyme: AE and monofunctional lyase: PGL
acetyltyrosyl pyruvate
-
competitive inhibition of PGL domain of full expressed enzyme: AE and monofunctional lyase: PGL
diethyl dicarbonate
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-
EGTA
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addition of 0.5-1 M reduces activity to 50%, Ca2+, Mn2+, Co2+ or Ni2+ restore activity
HCl
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0.5 M guanidinium HCl reduces activity to 28%
K2SO4
-
150 mM
KCl
-
150 mM
NaCl
-
150 mM
o-phenanthroline
-
-
phenylacetyl-alpha-hydroxy-Gly
-
competitive inhibition
Phenylglyoxal
-
-
Urea
-
addition of 1 M urea reduces activity to 58%
additional information
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.3
(R)-2-phenylbutyl-alpha-hydroxy-Gly
-
37C, pH 6.5
2.6
(R)-O-acetyl-mandelyl-alpha-hydroxyglycine
-
37C, pH 6.5
0.33
(S)-2-phenylbutyl-alpha-hydroxy-Gly
-
37C, pH 6.5
0.56
(S)-O-acetyl-mandelyl-alpha-hydroxyglycine
-
37C, pH 6.5
0.5
acetyl-D-Phe-alpha-hydroxyglycine
-
37C, pH 6.5
0.23
acetyl-L-Phe-alpha-hydroxyglycine
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37C, pH 6.5
0.013 - 0.238
alpha-N-Acetyl-Tyr-Val-alpha-hydroxyglycine
0.035 - 0.048
Dansyl-Tyr-Val-alpha-hydroxyglycine
-
37C, pH 7.0
0.0023 - 0.004
dansyl-Tyr-Val-Gly
-
37C, pH 6
0.0215 - 0.0887
N-2,4,6-trinitrophenyl-D-Tyr-L-Val-(S)-alpha-hydroxy-Gly
0.46
N-benzoyl-alpha-hydroxy-Gly
-
37C, pH 6.5
0.0102 - 0.33
Nalpha-Acetyl-Tyr-Val-alpha-hydroxyglycine
0.014 - 0.033
trinitrophenyl-D-Tyr-L-Val-alpha-hydroxy-Gly
additional information
additional information
apparent second-order rate constants at different pHs
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
3.2 - 25.7
N-2,4,6-trinitrophenyl-D-Tyr-L-Val-(S)-alpha-hydroxy-Gly
86 - 380
Nalpha-Acetyl-Tyr-Val-alpha-hydroxyglycine
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.31
(R)-2-phenylbutyl-alpha-hydroxy-Gly
-
37C, pH 6.5
0.28
(S)-2-phenylbutyl-alpha-hydroxy-Gly
-
37C, pH 6.5
3.2 - 4.8
acetylmethionyl pyruvate
0.049 - 0.071
acetylphenylalanyl pyruvate
0.55 - 0.92
acetyltyrosyl pyruvate
0.77
phenylacetyl-alpha-hydroxy-Gly
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37C, pH 6.5
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.25 - 0.32
-
dansyl-Tyr-Val-Gly as substrate
0.53
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Sephacryl S-300 purification step
4.5 - 8.3
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dansyl-Tyr-Val-alpha-hydroxyglycine as substrate
57.24
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affinity chromatography step II
510
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Mono Q pool A, after concentration
12000
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Superose 12 pool
23000
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PGL domain of full expressed enzyme: AE
76000
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PGL domain of transmembrane truncated enzyme: dAE
180000
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monofunctional lyase: PGL
16000000
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Mono Q fraction
additional information
-
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
25 - 37
assay at
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
-
enzyme is secreted into the medium from mouse C127 cells transfected with the rat MTC cDNA encoding the truncated type A enzyme
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
additional information
-
secretory granular fraction
-
Manually annotated by BRENDA team
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
38000
-
gel filtration
43900
monomer, secreted, rhodopsin-tagged protein, calculated from amino acid sequence
44400
monomer, secreted, rhodopsin-tagged protein, calculated from amino acid sequence
45000
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gel filtration
50000
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PAL domain, conversion of the 50000 MW form into a 43000 MW form occurs during gel filtration
53000
-
gel filtration
75000
-
truncated type A enzyme which catalyzes a two-step reaction involving an initial hydroxylation of peptidyl-Gly followed by conversion of the peptidyl-alpha-hydroxyglycine intermediate to the amidated product
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20C, 50% glycerol containing 1 mg/ml bovine serum albumin
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
enzyme is encoded by the intergranular domain of the PAM-encoding cDNA
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expression in a human embryonic kidney cell line that lacks regulated secretory granules
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expression in Chinese hamster ovary cells
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expression in chinese hamster ovary K-1 cells
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expression in cultured Sf9 insect cells
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
D590N
-
no secretion
D599N
-
no secretion
D652N
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no secretion
D705N
-
much less secretion and less active than wild-type
E707Q
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much less secretion than wild-type
H532A
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no secretion
H585A
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less active than wild-type
H603A
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no secretion
H690A
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less active than wild-type
H697A
-
no changes in secretion an activity
H786A
-
less active than wild-type
H817A
-
no changes in secretion an activity