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Information on EC 4.3.2.5 - peptidylamidoglycolate lyase
for references in articles please use BRENDA:EC4.3.2.5
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EC Tree 4 Lyases
4.3 Carbon-nitrogen lyases
4.3.2 Amidine-lyases
4.3.2.5 peptidylamidoglycolate lyase
IUBMB Comments
Requires zinc. 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. In mammals, the two activities are part of a bifunctional protein.
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
- 4.3.2.5
-
glycine-extended
- monooxygenase
-
alpha-hydroxylating
- ascorbate
- neuropeptides
-
1.14.17.3
-
entails
-
alpha-monooxygenase
- alpha-ae
-
peptidyl-alpha-hydroxyglycine
-
4-phenyl-3-butenoic
-
dealkylation
-
prohormones
- pro-peptide
-
ascorbate-dependent
-
miller
showSynonyms
peptidylamidoglycolate lyase, bifunctional peptidylglycine alpha-amidating enzyme, alpha-hydroxyglycine amidating dealkylase, more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
alpha-hydroxyglycine amidating dealkylase
-
-
-
-
lyase, peptidyl-alpha hydroxyglycine
-
-
-
-
PAL
PALm
peptidyl-alpha-hydroxyglycine alpha-amidating lyase
peptidyl-alpha-hydroxyglycine alpha-amidating lyase
-
-
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
[peptide]-(2S)-2-hydroxyglycine = [peptide]-amide + glyoxylate
-
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
amidine-lyase reaction
-
-
-
-
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SYSTEMATIC NAME
IUBMB Comments
[peptide]-(2S)-2-hydroxyglycine peptidyl-amide-lyase (glyoxylate-forming)
Requires zinc. 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. In mammals, the two activities are part of a bifunctional protein.
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CAS REGISTRY NUMBER
COMMENTARY
131689-50-4
-
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
(R)-2-phenylbutyl-alpha-hydroxy-Gly
(R)-2-phenylbutyl-NH2 + glyoxylate
-
Substrates: -
Products: -
Products: -
?
(R)-O-acetyl-mandelyl-alpha-hydroxyglycine
(R)-O-acetyl-mandelyl-NH2 + glyoxylate
-
Substrates: -
Products: -
Products: -
?
(S)-2-phenylbutyl-alpha-hydroxy-Gly
(S)-2-phenylbutyl-NH2 + glyoxylate
-
Substrates: -
Products: -
Products: -
?
(S)-N-dansyl-Tyr-Val-alpha-hydroxyglycine
N-dansyl-Tyr-Val-NH2 + glyoxylate
Substrates: -
Products: -
Products: -
?
(S)-O-acetyl-mandelyl-alpha-hydroxyglycine
(S)-O-acetyl-mandelyl-NH2 + glyoxylate
-
Substrates: -
Products: -
Products: -
?
acetyl-D-Phe-alpha-hydroxyglycine
acetyl-D-Phe-NH2 + glyoxylate
-
Substrates: -
Products: -
Products: -
?
acetyl-L-Phe-alpha-hydroxyglycine
acetyl-L-Phe-NH2 + glyoxylate
-
Substrates: -
Products: -
Products: -
?
dansyl-Tyr-Val-alpha-hydroxyglycine
dansyl-Tyr-Val-NH2 + glyoxylate
-
Substrates: -
Products: -
Products: -
?
dansyl-Tyr-Val-Gly
dansyl-Tyr-Val-NH2 + glyoxylate
-
Substrates: -
Products: -
Products: -
?
N-2,4,6-trinitrophenyl-D-Tyr-L-Val-(S)-alpha-hydroxy-Gly
N-2,4,6-trinitrophenyl-D-Tyr-L-Val-amide + glyoxylate
Substrates: -
Products: -
Products: -
?
trinitrophenyl-D-Tyr-Val-alpha-hydroxy-Gly
trinitrophenyl-D-Tyr-Val-NH2 + glyoxylate
-
Substrates: -
Products: -
Products: -
?
alpha-hydroxyglycine-extended peptide
peptidyl amide + glyoxylate
-
Substrates: -
Products: -
Products: -
?
alpha-hydroxyglycine-extended peptide
peptidyl amide + glyoxylate
-
Substrates: the alpha-hydroxyglycine moiety produced by EC 1.14.17.3 is of the S configuration
Products: -
Products: -
?
alpha-hydroxyglycine-extended peptide
peptidyl amide + glyoxylate
-
Substrates: -
Products: -
Products: -
?
alpha-hydroxyglycine-extended peptide
peptidyl amide + glyoxylate
-
Substrates: -
Products: -
Products: -
?
alpha-N-acetyl-Tyr-Val-alpha-hydroxyglycine
alpha-N-acetyl-Tyr-Val-NH2 + glyoxylate
Substrates: -
Products: -
Products: -
?
alpha-N-acetyl-Tyr-Val-alpha-hydroxyglycine
alpha-N-acetyl-Tyr-Val-NH2 + glyoxylate
Substrates: -
Products: -
Products: -
?
Nalpha-acetyl-Tyr-Val-alpha-hydroxyglycine
Nalpha-acetyl-Tyr-Val-NH2 + glyoxylate
-
Substrates: -
Products: -
Products: -
?
Nalpha-acetyl-Tyr-Val-alpha-hydroxyglycine
Nalpha-acetyl-Tyr-Val-NH2 + glyoxylate
-
Substrates: -
Products: -
Products: -
?
peptidylamidoglycolate
peptidyl amide + glyoxylate
Substrates: -
Products: -
Products: -
?
peptidylamidoglycolate
peptidyl amide + glyoxylate
-
Substrates: -
Products: -
Products: -
?
peptidylamidoglycolate
peptidyl amide + glyoxylate
-
Substrates: -
Products: -
Products: -
?
peptidylamidoglycolate
peptidyl amide + glyoxylate
Substrates: -
Products: -
Products: -
?
trinitrophenyl-D-Tyr-L-Val-alpha-hydroxy-Gly
trinitrophenyl-D-Tyr-L-Val-NH2 + glyoxylate
-
Substrates: -
Products: -
Products: -
?
trinitrophenyl-D-Tyr-L-Val-alpha-hydroxy-Gly
trinitrophenyl-D-Tyr-L-Val-NH2 + glyoxylate
-
Substrates: -
Products: -
Products: -
?
[peptide]-(2S)-2-hydroxyglycine
[peptide]-amide + glyoxylate
Anuroctonus pococki subsp. bajae
-
Substrates: -
Products: -
Products: -
?
[peptide]-(2S)-2-hydroxyglycine
[peptide]-amide + glyoxylate
-
Substrates: -
Products: -
Products: -
?
[peptide]-(2S)-2-hydroxyglycine
[peptide]-amide + glyoxylate
-
Substrates: -
Products: -
Products: -
?
[peptide]-(2S)-2-hydroxyglycine
[peptide]-amide + glyoxylate
-
Substrates: -
Products: -
Products: -
?
[peptide]-(2S)-2-hydroxyglycine
[peptide]-amide + glyoxylate
-
Substrates: -
Products: -
Products: -
?
[peptide]-(2S)-2-hydroxyglycine
[peptide]-amide + glyoxylate
-
Substrates: -
Products: -
Products: -
?
[peptide]-(2S)-2-hydroxyglycine
[peptide]-amide + glyoxylate
Centruroides orizaba
-
Substrates: -
Products: -
Products: -
?
[peptide]-(2S)-2-hydroxyglycine
[peptide]-amide + glyoxylate
-
Substrates: -
Products: -
Products: -
?
[peptide]-(2S)-2-hydroxyglycine
[peptide]-amide + glyoxylate
-
Substrates: -
Products: -
Products: -
?
[peptide]-(2S)-2-hydroxyglycine
[peptide]-amide + glyoxylate
-
Substrates: -
Products: -
Products: -
?
[peptide]-(2S)-2-hydroxyglycine
[peptide]-amide + glyoxylate
-
Substrates: -
Products: -
Products: -
?
[peptide]-(2S)-2-hydroxyglycine
[peptide]-amide + glyoxylate
-
Substrates: -
Products: -
Products: -
?
[peptide]-(2S)-2-hydroxyglycine
[peptide]-amide + glyoxylate
-
Substrates: -
Products: -
Products: -
?
[peptide]-(2S)-2-hydroxyglycine
[peptide]-amide + glyoxylate
-
Substrates: -
Products: -
Products: -
?
[peptide]-(2S)-2-hydroxyglycine
[peptide]-amide + glyoxylate
-
Substrates: -
Products: -
Products: -
?
[peptide]-(2S)-2-hydroxyglycine
[peptide]-amide + glyoxylate
-
Substrates: -
Products: -
Products: -
?
[peptide]-(2S)-2-hydroxyglycine
[peptide]-amide + glyoxylate
-
Substrates: -
Products: -
Products: -
?
[peptide]-(2S)-2-hydroxyglycine
[peptide]-amide + glyoxylate
-
Substrates: -
Products: -
Products: -
?
[peptide]-(2S)-2-hydroxyglycine
[peptide]-amide + glyoxylate
-
Substrates: -
Products: -
Products: -
?
[peptide]-(2S)-2-hydroxyglycine
[peptide]-amide + glyoxylate
-
Substrates: -
Products: -
Products: -
?
[peptide]-(2S)-2-hydroxyglycine
[peptide]-amide + glyoxylate
-
Substrates: -
Products: -
Products: -
?
[peptide]-(2S)-2-hydroxyglycine
[peptide]-amide + glyoxylate
-
Substrates: -
Products: -
Products: -
?
additional information
?
-
-
Substrates: in the amidation reaction, the reactant (glycine-extended peptide) is converted into a reaction intermediate (hydroxyglycine-extended peptide) by the copper-dependent peptidylglycine-alpha-hydroxylating monooxygenase (PHM) domain of PAM. The hydroxyglycine-extended peptide is then converted into amidated product by the peptidyl-alpha-hydroxyglycine alpha-amidating lyase (PAL) domain of PAM
Products: -
Products: -
?
additional information
?
-
-
Substrates: in the amidation reaction, the reactant (glycine-extended peptide) is converted into a reaction intermediate (hydroxyglycine-extended peptide) by the copper-dependent peptidylglycine-alpha-hydroxylating monooxygenase (PHM) domain of PAM. The hydroxyglycine-extended peptide is then converted into amidated product by the peptidyl-alpha-hydroxyglycine alpha-amidating lyase (PAL) domain of PAM
Products: -
Products: -
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
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
Substrates: -
Products: -
Products: -
?
peptidylamidoglycolate
peptidyl amide + glyoxylate
Substrates: -
Products: -
Products: -
?
peptidylamidoglycolate
peptidyl amide + glyoxylate
-
Substrates: -
Products: -
Products: -
?
peptidylamidoglycolate
peptidyl amide + glyoxylate
-
Substrates: -
Products: -
Products: -
?
peptidylamidoglycolate
peptidyl amide + glyoxylate
Substrates: -
Products: -
Products: -
?
[peptide]-(2S)-2-hydroxyglycine
[peptide]-amide + glyoxylate
Anuroctonus pococki subsp. bajae
-
Substrates: -
Products: -
Products: -
?
[peptide]-(2S)-2-hydroxyglycine
[peptide]-amide + glyoxylate
-
Substrates: -
Products: -
Products: -
?
[peptide]-(2S)-2-hydroxyglycine
[peptide]-amide + glyoxylate
-
Substrates: -
Products: -
Products: -
?
[peptide]-(2S)-2-hydroxyglycine
[peptide]-amide + glyoxylate
-
Substrates: -
Products: -
Products: -
?
[peptide]-(2S)-2-hydroxyglycine
[peptide]-amide + glyoxylate
-
Substrates: -
Products: -
Products: -
?
[peptide]-(2S)-2-hydroxyglycine
[peptide]-amide + glyoxylate
-
Substrates: -
Products: -
Products: -
?
[peptide]-(2S)-2-hydroxyglycine
[peptide]-amide + glyoxylate
Centruroides orizaba
-
Substrates: -
Products: -
Products: -
?
[peptide]-(2S)-2-hydroxyglycine
[peptide]-amide + glyoxylate
-
Substrates: -
Products: -
Products: -
?
[peptide]-(2S)-2-hydroxyglycine
[peptide]-amide + glyoxylate
-
Substrates: -
Products: -
Products: -
?
[peptide]-(2S)-2-hydroxyglycine
[peptide]-amide + glyoxylate
-
Substrates: -
Products: -
Products: -
?
[peptide]-(2S)-2-hydroxyglycine
[peptide]-amide + glyoxylate
-
Substrates: -
Products: -
Products: -
?
[peptide]-(2S)-2-hydroxyglycine
[peptide]-amide + glyoxylate
-
Substrates: -
Products: -
Products: -
?
[peptide]-(2S)-2-hydroxyglycine
[peptide]-amide + glyoxylate
-
Substrates: -
Products: -
Products: -
?
[peptide]-(2S)-2-hydroxyglycine
[peptide]-amide + glyoxylate
-
Substrates: -
Products: -
Products: -
?
[peptide]-(2S)-2-hydroxyglycine
[peptide]-amide + glyoxylate
-
Substrates: -
Products: -
Products: -
?
[peptide]-(2S)-2-hydroxyglycine
[peptide]-amide + glyoxylate
-
Substrates: -
Products: -
Products: -
?
[peptide]-(2S)-2-hydroxyglycine
[peptide]-amide + glyoxylate
-
Substrates: -
Products: -
Products: -
?
[peptide]-(2S)-2-hydroxyglycine
[peptide]-amide + glyoxylate
-
Substrates: -
Products: -
Products: -
?
[peptide]-(2S)-2-hydroxyglycine
[peptide]-amide + glyoxylate
-
Substrates: -
Products: -
Products: -
?
[peptide]-(2S)-2-hydroxyglycine
[peptide]-amide + glyoxylate
-
Substrates: -
Products: -
Products: -
?
[peptide]-(2S)-2-hydroxyglycine
[peptide]-amide + glyoxylate
-
Substrates: -
Products: -
Products: -
?
[peptide]-(2S)-2-hydroxyglycine
[peptide]-amide + glyoxylate
-
Substrates: -
Products: -
Products: -
?
additional information
?
-
-
Substrates: in the amidation reaction, the reactant (glycine-extended peptide) is converted into a reaction intermediate (hydroxyglycine-extended peptide) by the copper-dependent peptidylglycine-alpha-hydroxylating monooxygenase (PHM) domain of PAM. The hydroxyglycine-extended peptide is then converted into amidated product by the peptidyl-alpha-hydroxyglycine alpha-amidating lyase (PAL) domain of PAM
Products: -
Products: -
?
additional information
?
-
-
Substrates: in the amidation reaction, the reactant (glycine-extended peptide) is converted into a reaction intermediate (hydroxyglycine-extended peptide) by the copper-dependent peptidylglycine-alpha-hydroxylating monooxygenase (PHM) domain of PAM. The hydroxyglycine-extended peptide is then converted into amidated product by the peptidyl-alpha-hydroxyglycine alpha-amidating lyase (PAL) domain of PAM
Products: -
Products: -
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Cd2+
Co2+
Zn2+
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
Cd2+
activates, binding of Co2+ or Cd2+ to empty zinc-binding sites on PAL
Co2+
activates, binding of Co2+ or Cd2+ to empty zinc-binding sites on PAL
Zn2+
activates, binding of Co2+ or Cd2+ to empty zinc-binding sites on PAL
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
acetylmethionyl pyruvate
-
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
EGTA
-
addition of 0.5-1 M reduces activity to 50%, Ca2+, Mn2+, Co2+ or Ni2+ restore activity
EDTA
-
addition of 0.5-1 M reduces activity to 50%, Ca2+, Mn2+, Co2+ or Ni2+ restore activity
additional information
-
the inhibitors of PAM: acetyl-L-Phe-acetic acid and [(4-methoxybenzoyl)oxy]acetic acid show no effect of the KM of the monofunctional lyase: PGL
-
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
apparent second-order rate constants at different pHs
-
0.0215
N-2,4,6-trinitrophenyl-D-Tyr-L-Val-(S)-alpha-hydroxy-Gly
pH 6.0, 25°C, wild-type enzyme
0.0887
N-2,4,6-trinitrophenyl-D-Tyr-L-Val-(S)-alpha-hydroxy-Gly
pH 6.0, 25°C, metal-depleted enzyme
0.0139
Nalpha-Acetyl-Tyr-Val-alpha-hydroxyglycine
-
37°C, pH 5.5, recombinant wild-type
0.034
Nalpha-Acetyl-Tyr-Val-alpha-hydroxyglycine
-
37°C, pH 7.4, with endoprotease Arg-C digested PAM-3 protein
0.037
Nalpha-Acetyl-Tyr-Val-alpha-hydroxyglycine
-
37°C, pH 7.4, undigested PAM-3 protein
0.014
trinitrophenyl-D-Tyr-L-Val-alpha-hydroxy-Gly
-
37°C, pH 6.6, PGL domain of transmembrane truncated enzyme: dAE
0.018
trinitrophenyl-D-Tyr-L-Val-alpha-hydroxy-Gly
-
37°C, pH 6.6, PGL domain of full expressed enzyme: AE
0.019
trinitrophenyl-D-Tyr-L-Val-alpha-hydroxy-Gly
-
37°C, pH 6.6, monofunctional lyase: PGL
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
3.2
N-2,4,6-trinitrophenyl-D-Tyr-L-Val-(S)-alpha-hydroxy-Gly
pH 6.0, 25°C, metal-depleted enzyme
25.7
N-2,4,6-trinitrophenyl-D-Tyr-L-Val-(S)-alpha-hydroxy-Gly
pH 6.0, 25°C, wild-type enzyme
86
Nalpha-Acetyl-Tyr-Val-alpha-hydroxyglycine
-
37°C, pH 7.4, with endoprotease Arg-C digested PAM-3 protein
92
Nalpha-Acetyl-Tyr-Val-alpha-hydroxyglycine
-
37°C, pH 7.4, undigested PAM-3 protein
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
4.8
acetylmethionyl pyruvate
-
37°C, pH 6.6, PGL domain of full expressed enzyme: AE
0.071
acetylphenylalanyl pyruvate
-
37°C, pH 6.6, PGL domain of full expressed enzyme: AE
0.92
acetyltyrosyl pyruvate
-
37°C, pH 6.6, PGL domain of full expressed enzyme: AE
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
37
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
EC 1.14.17.3 (PHM) and EC 4.3.2.5 (PAL) are part of a bifunctional protein
-
-
brenda
bifunctional peptidylglycine alpha-amidating enzyme
SwissProt
brenda
expression in COS-7 cells, the two enzymes EC 1.14.17.3 and EC 4.3.2.5 are generated from a common precursor protein encoded by a single mRNA
-
-
brenda
soluble, bifunctional form PAM-3, expression in a human embryonic kidney cell line that lacks regulated secretory granules, EC 1.14.17.3 and EC 4.3.2.5 are contained within the bifunctional peptidylglycine alpha-amidation monooxygenase, PAM
-
-
brenda
Sprague-Dawley, EC 1.14.17.3 (PHM) and EC 4.3.2.5 (PAL) are part of a bifunctional, integral membrane protein precursor, peptidylglycine alpha-amidating monooxygenase, PAM, which consists of independent catalytic domains separated from each other and from the putative transmembrane domain by flexible regions accessible to attack by a wide variety of endoproteinases
-
-
brenda
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, enzyme is secreted into the medium from mouse C127 cells transfected with the rat MTC cDNA encoding the truncated type A enzyme
-
-
brenda
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
enzyme is secreted into the medium from mouse C127 cells transfected with the rat MTC cDNA encoding the truncated type A enzyme
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
Highest Expressing Human Cell Lines
Cell Line LinksPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
-
the the peptidyl-alpha-hydroxyglycine alpha-amidating lyase (PAL) is located on a domain of peptidylglycine alpha-amidating monooxygenase (PAM). The monooxygenase reaction is a slower step in peptide amidation, so that in peptidylglycine alpha-amidating monooxygenase (PAM) deficient mice, peptidyl-alpha-hydroxyglycine alpha-amidating lyase becomes the limiting factor of conversion of amidated peptides, overview. Peptidylglycine-alpha-hydroxylating monooxygenase, PHM, and peptidyl-alpha-hydroxyglycine alpha-amidating lyase, PAL, are stitched together in most vertebrates, kinetic studies with purified PHM and PAL revealed a higher affinity of PHM for its peptide substrate and a higher turnover number for PAL
additional information
-
the the peptidyl-alpha-hydroxyglycine alpha-amidating lyase (PAL) is located on a domain of peptidylglycine alpha-amidating monooxygenase (PAM). The monooxygenase reaction is a slower step in peptide amidation, so that in peptidylglycine alpha-amidating monooxygenase (PAM) deficient mice, peptidyl-alpha-hydroxyglycine alpha-amidating lyase becomes the limiting factor of conversion of amidated peptides, overview. Peptidylglycine-alpha-hydroxylating monooxygenase, PHM, and peptidyl-alpha-hydroxyglycine alpha-amidating lyase, PAL, are stitched together in most vertebrates, kinetic studies with purified PHM and PAL revealed a higher affinity of PHM for its peptide substrate and a higher turnover number for PAL
-
Show AA Sequence and Transmembrane Helices (938 entries)
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
43900
monomer, secreted, rhodopsin-tagged protein, calculated from amino acid sequence
44400
monomer, secreted, rhodopsin-tagged protein, calculated from amino acid sequence
50000
-
PAL domain, conversion of the 50000 MW form into a 43000 MW form occurs during 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
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in a human embryonic kidney cell line that lacks regulated secretory granules
-
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Perkins, S.N.; Husten, E.J.; Eipper, B.A.
The 108-kDA peptidylglycine alpha-amidating monooxygenase precursor contains two separable enzymatic activities involved in peptide amidation
Biochem. Biophys. Res. Commun.
171
926-932
1990
Bos taurus
brenda
Suzuki, K.; Shimoi, H.; Iwasaki, Y.; Kawahara, T.; Matsuura, Y.; Nishikawa, Y.
Elucidation of amidating reaction mechanism by frog amidating enzyme, peptidylglycine alpha-hydroxylating monooxygenase, expressed in insect cell culture
EMBO J.
9
4259-4265
1990
Xenopus laevis
brenda
Merkler, D.J.; Young, S.D.
Recombinant type A rat 75-kDa alpha-amidating enzyme catalyzes the conversion of glycine-extended peptides to peptide amides via an alpha-hydroxyglycine intermediate
Arch. Biochem. Biophys.
289
192-196
1991
Rattus norvegicus
brenda
Bell, J.; Ash, D.E.; Snyder, L.M.; Kulathila, R.; Blackburn, N.J.; Merkler, D.J.
Structural and functional investigations on the role of zinc in bifunctional rat peptidylglycine alpha-amidating enzyme
Biochemistry
36
16239-16246
1997
Rattus norvegicus (P14925)
brenda
Ping, D.; Mounier, C.E.; May, S.W.
Reaction versus subsite stereospecificity of peptidylglycine alpha-monooxygenase and peptidylamidoglycolate lyase, the two enzymes involved in peptide amidation
J. Biol. Chem.
270
29250-29255
1995
Bos taurus
brenda
Francisco, W.A.; Merkler, D.J.; Blackburn, N.J.; Klinman, J.P.
Kinetic mechanism and intrinsic isotope effects for the peptidylglycine alpha-amidating enzyme reaction
Biochemistry
37
8244-8252
1998
Rattus norvegicus
brenda
Katopodis, A.G.; Ping, D.; May, S.W.
A novel enzyme from bovine neurointermediate pituitary catalyzes dealkylation of alpha-hydroxyglycine derivatives, thereby functioning sequentially with peptidylglycine alpha-amidating monooxygenase in peptideamidation
Biochemistry
29
6115-6120
1990
Bos taurus
brenda
Katopodis, A.G.; Ping, D.; Smith, C.E.; May, S.W.
Functional and structural characterization of peptidylamidoglycolate lyase, the enzyme catalyzing the second step in peptide amidation
Biochemistry
30
6189-6194
1991
Bos taurus
brenda
Husten, E.J.; Tausk, F.A.; Keutmann, H.T.; Eipper, B.A.
Use of endoproteases to identify catalytic domains, linker regions, and functional interactions in soluble peptidylglycine alpha-amidating monooxygenase
J. Biol. Chem.
268
9709-9717
1993
Bos taurus, Rattus norvegicus
brenda
Ping, D.; Katopodis, A.G.; May, S.W.
Tandem stereochemistry of peptidylglycine alpha-monooxygenase and peptidylamidoglycolate lyase, the two enzymes involved in peptide amidation
J. Am. Chem. Soc.
114
3998-4000
1992
Bos taurus
-
brenda
Husten, E.J.; Eipper, B.A.
The membrane-bound bifunctional peptidylglycine alpha-amidating monooxygenase protein. Exploration of its domain structure through limited proteolysis.
J. Biol. Chem.
266
17004-17010
1991
Rattus norvegicus
brenda
Eipper, B.A.; Perkins, S.N.; Husten, E.J.; Johnson, R.C.; Keutmann, H.T.; Mains, R.E.
Peptidyl-alpha-hydroxyglycine alpha-amidating lyase. Purification, characterization, and expressio
J. Biol. Chem.
266
7827-7833
1991
Bos taurus
brenda
Takahashi, K.; Okamoto, H.; Seino, H.; Noguchi, M.
Peptidylglycine alpha-amidating reaction: evidence for a two-step mechanism involving a stable intermediate at neutral pH
Biochem. Biophys. Res. Commun.
169
524-530
1990
Bos taurus, Rattus norvegicus
brenda
Kato, I.; Yonekura, H.; Tajima, M.; Yanagi, M.; Yamamoto, H.; Okamoto, H.
Two enzymes concerned in peptide hormone alpha-amidation are synthesized from a single mRN
Biochem. Biophys. Res. Commun.
172
197-203
1990
Rattus norvegicus
brenda
Satani, M.; Takahashi, K.; Sakamoto, H.; Harada, S.; Kaida, Y.; Noguchi, M.
Expression and characterization of human bifunctional peptidylglycine alpha-amidating monooxygenase
Protein Expr. Purif.
28
293-302
2003
Homo sapiens
brenda
Kolhekar, A.S.; Bell, J.; Shiozaki, E.N.; Jin, L.; Keutmann, H.T.; Hand, T.A.; Mains, R.E.; Eipper, B.A.
Essential features of the catalytic core of peptidyl-a-hydroxyglycine alpha-amidating Lyase
Biochemistry
41
12384-12394
2002
Rattus norvegicus
brenda
Moore, A.B.; May, S.W.
Kinetic and inhibition studies on substrate channelling in the bifunctional enzyme catalysing C-terminal amidation
Biochem. J.
341
33-40
1999
Bos taurus, Xenopus laevis
brenda
Garmendia, O.; Rodriguez, M.P.; Burrell, M.A.; Villaro, A.C.
Immunocytochemical finding of the amidating enzymes in mouse pancreatic A-, B-, and D-cells: a comparison with human and rat
J. Histochem. Cytochem.
50
1401-1415
2002
Homo sapiens, Mus musculus, Rattus norvegicus
brenda
Park, D.; Han, M.; Kim, Y.C.; Han, K.A.; Taghert, P.H.
Ap-let neurons-a peptidergic circuit potentially controlling ecdysial behavior in Drosophila
Dev. Biol.
269
95-108
2004
Drosophila melanogaster (Q9W1L5)
brenda
Han, M.; Park, D.; Vanderzalm, P.J.; Mains, R.E.; Eipper, B.A.; Taghert, P.H.
Drosophila uses two distinct neuropeptide amidating enzymes, dPAL1 and dPAL2
J. Neurochem.
90
129-141
2004
Drosophila melanogaster (Q9V5E1), Drosophila melanogaster (Q9W1L5), Rattus norvegicus (P14925)
brenda
Takahashi, K.; Harada, S.; Higashimoto, Y.; Shimokawa, C.; Sato, H.; Sugishima, M.; Kaida, Y.; Noguchi, M.
Involvement of metals in enzymatic and nonenzymatic decomposition of C-terminal alpha-hydroxyglycine to amide: An implication for the catalytic role of enzyme-bound zinc in the peptidylamidoglycolate lyase reaction
Biochemistry
48
1654-1662
2009
Homo sapiens (P19021)
brenda
Yin, P.; Bousquet-Moore, D.; Annangudi, S.P.; Southey, B.R.; Mains, R.E.; Eipper, B.A.; Sweedler, J.V.
Probing the production of amidated peptides following genetic and dietary copper manipulations
PLoS ONE
6
e28679
2011
Mus musculus, Mus musculus C57/BL6J
brenda
Delgado-Prudencio, G.; Possani, L.D.; Becerril, B.; Ortiz, E.
The dual alpha-amidation system in scorpion venom glands
Toxins
11
425
2019
Anuroctonus pococki subsp. bajae, Centruroides hentzi, Centruroides hirsutipalpus, Centruroides limpidus, Centruroides noxius, Centruroides ochraceus, Centruroides orizaba, Centruroides sculpturatus, Chihuahuanus coahuilae, Diplocentrus melici, Hadrurus concolorous, Hoffmannihadrurus aztecus, Leiurus abdullahbayrami, Megacormus gertschi, Olivierus martensii, Pandinus imperator, Paravaejovis schwenkmeyeri, Serradigitus gertschi, Superstitionia donensis, Thorellius cristimanus, Tityus trivittatus, Urodacus yaschenkoi
brenda
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