Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
(R)-2-phenylbutyl-alpha-hydroxy-Gly
(R)-2-phenylbutyl-NH2 + glyoxylate
-
-
-
-
?
(R)-O-acetyl-mandelyl-alpha-hydroxyglycine
(R)-O-acetyl-mandelyl-NH2 + glyoxylate
-
-
-
-
?
(S)-2-phenylbutyl-alpha-hydroxy-Gly
(S)-2-phenylbutyl-NH2 + glyoxylate
-
-
-
-
?
(S)-N-dansyl-Tyr-Val-alpha-hydroxyglycine
N-dansyl-Tyr-Val-NH2 + glyoxylate
-
-
-
?
(S)-O-acetyl-mandelyl-alpha-hydroxyglycine
(S)-O-acetyl-mandelyl-NH2 + glyoxylate
-
-
-
-
?
acetyl-D-Phe-alpha-hydroxyglycine
acetyl-D-Phe-NH2 + glyoxylate
-
-
-
-
?
acetyl-L-Phe-alpha-hydroxyglycine
acetyl-L-Phe-NH2 + glyoxylate
-
-
-
-
?
alpha-hydroxybenzoylglycine
benzamide + glyoxylate
-
-
-
-
?
alpha-hydroxyglycine-extended peptide
peptidyl amide + glyoxylate
alpha-N-acetyl-Tyr-Val-alpha-hydroxyglycine
alpha-N-acetyl-Tyr-Val-NH2 + glyoxylate
dansyl-Tyr-Val-alpha-hydroxyglycine
dansyl-Tyr-Val-NH2 + glyoxylate
-
-
-
?
dansyl-Tyr-Val-Gly
dansyl-Tyr-Val-NH2 + glyoxylate
-
-
-
-
?
N-2,4,6-trinitrophenyl-D-Tyr-L-Val-(S)-alpha-hydroxy-Gly
N-2,4,6-trinitrophenyl-D-Tyr-L-Val-amide + glyoxylate
-
-
-
?
N-benzoyl-alpha-hydroxy-Gly
benzamide + glyoxylate
-
-
-
-
?
Nalpha-acetyl-Tyr-Val-alpha-hydroxyglycine
Nalpha-acetyl-Tyr-Val-NH2 + glyoxylate
peptidylamidoglycolate
peptidyl amide + glyoxylate
trinitrophenyl-D-Tyr-L-Val-alpha-hydroxy-Gly
trinitrophenyl-D-Tyr-L-Val-NH2 + glyoxylate
trinitrophenyl-D-Tyr-Val-alpha-hydroxy-Gly
trinitrophenyl-D-Tyr-Val-NH2 + glyoxylate
-
-
-
?
additional information
?
-
alpha-hydroxyglycine-extended peptide
peptidyl amide + glyoxylate
-
-
-
-
?
alpha-hydroxyglycine-extended peptide
peptidyl amide + glyoxylate
-
-
-
?
alpha-hydroxyglycine-extended peptide
peptidyl amide + glyoxylate
-
-
-
-
?
alpha-hydroxyglycine-extended peptide
peptidyl amide + glyoxylate
-
the alpha-hydroxyglycine moiety produced by EC 1.14.17.3 is of the S configuration
-
-
?
alpha-hydroxyglycine-extended peptide
peptidyl amide + glyoxylate
-
-
-
-
?
alpha-hydroxyglycine-extended peptide
peptidyl amide + glyoxylate
-
-
-
?
alpha-N-acetyl-Tyr-Val-alpha-hydroxyglycine
alpha-N-acetyl-Tyr-Val-NH2 + glyoxylate
-
-
-
?
alpha-N-acetyl-Tyr-Val-alpha-hydroxyglycine
alpha-N-acetyl-Tyr-Val-NH2 + glyoxylate
-
-
-
?
Nalpha-acetyl-Tyr-Val-alpha-hydroxyglycine
Nalpha-acetyl-Tyr-Val-NH2 + glyoxylate
-
-
-
-
?
Nalpha-acetyl-Tyr-Val-alpha-hydroxyglycine
Nalpha-acetyl-Tyr-Val-NH2 + glyoxylate
-
-
-
-
?
Nalpha-acetyl-Tyr-Val-alpha-hydroxyglycine
Nalpha-acetyl-Tyr-Val-NH2 + glyoxylate
-
-
-
?
Nalpha-acetyl-Tyr-Val-alpha-hydroxyglycine
Nalpha-acetyl-Tyr-Val-NH2 + glyoxylate
-
-
-
-
?
peptidylamidoglycolate
peptidyl amide + glyoxylate
-
-
-
?
peptidylamidoglycolate
peptidyl amide + glyoxylate
-
-
-
-
?
peptidylamidoglycolate
peptidyl amide + glyoxylate
-
-
-
-
?
peptidylamidoglycolate
peptidyl amide + glyoxylate
-
-
-
?
trinitrophenyl-D-Tyr-L-Val-alpha-hydroxy-Gly
trinitrophenyl-D-Tyr-L-Val-NH2 + glyoxylate
-
-
-
-
?
trinitrophenyl-D-Tyr-L-Val-alpha-hydroxy-Gly
trinitrophenyl-D-Tyr-L-Val-NH2 + glyoxylate
-
-
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
-
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
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
0.3
(R)-2-phenylbutyl-alpha-hydroxy-Gly
-
37°C, pH 6.5
2.6
(R)-O-acetyl-mandelyl-alpha-hydroxyglycine
-
37°C, pH 6.5
0.33
(S)-2-phenylbutyl-alpha-hydroxy-Gly
-
37°C, pH 6.5
0.56
(S)-O-acetyl-mandelyl-alpha-hydroxyglycine
-
37°C, pH 6.5
0.5
acetyl-D-Phe-alpha-hydroxyglycine
-
37°C, pH 6.5
0.23
acetyl-L-Phe-alpha-hydroxyglycine
-
37°C, pH 6.5
0.013 - 0.238
alpha-N-Acetyl-Tyr-Val-alpha-hydroxyglycine
0.035 - 0.048
Dansyl-Tyr-Val-alpha-hydroxyglycine
-
37°C, pH 7.0
0.0023 - 0.004
dansyl-Tyr-Val-Gly
-
37°C, 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
-
37°C, 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
-
0.013
alpha-N-Acetyl-Tyr-Val-alpha-hydroxyglycine
-
0.045
alpha-N-Acetyl-Tyr-Val-alpha-hydroxyglycine
-
0.238
alpha-N-Acetyl-Tyr-Val-alpha-hydroxyglycine
-
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
0.0102
Nalpha-Acetyl-Tyr-Val-alpha-hydroxyglycine
-
37°C, pH 5.5, E707Q
0.0139
Nalpha-Acetyl-Tyr-Val-alpha-hydroxyglycine
-
37°C, pH 5.5, recombinant wild-type
0.0156
Nalpha-Acetyl-Tyr-Val-alpha-hydroxyglycine
-
37°C, pH 5.5, H690A
0.0214
Nalpha-Acetyl-Tyr-Val-alpha-hydroxyglycine
-
37°C, pH 5.5, D705N
0.0231
Nalpha-Acetyl-Tyr-Val-alpha-hydroxyglycine
-
37°C, pH 5.5, H585A
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
0.038
Nalpha-Acetyl-Tyr-Val-alpha-hydroxyglycine
-
37°C, pH 7
0.0985
Nalpha-Acetyl-Tyr-Val-alpha-hydroxyglycine
-
37°C, pH 5.5, H786A
0.33
Nalpha-Acetyl-Tyr-Val-alpha-hydroxyglycine
-
37°C, pH 5.5
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
0.027
trinitrophenyl-D-Tyr-L-Val-alpha-hydroxy-Gly
-
37°C, pH 6.5
0.033
trinitrophenyl-D-Tyr-L-Val-alpha-hydroxy-Gly
-
37°C, pH 6.6
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
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
Rattus norvegicus (P14925), Drosophila melanogaster (Q9V5E1), Drosophila melanogaster (Q9W1L5)
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
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