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Information on EC 4.3.2.5 - peptidylamidoglycolate lyase and Organism(s) Homo sapiens and UniProt Accession P19021

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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
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.
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This record set is specific for:
Homo sapiens
UNIPROT: P19021
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Word Map
  • 4.3.2.5
  • peptidylglycine
  • alpha-hydroxylating
  • neuropeptides
  • alpha-amidating
  • glycine-extended
  • 1.14.17.3
  • ascorbate
  • alpha-monooxygenase
  • entails
  • peptidyl-alpha-hydroxyglycine
  • 4-phenyl-3-butenoic
  • pro-peptide
  • mechanism-based
  • ascorbate-dependent
  • gene-related
  • olefinic
  • turnover-dependent
  • tautomer
  • enol
  • monofunctional
  • carrageenan-induced
  • miller
  • chiralpak
  • dealkylation
  • copper-dependent
  • diketo
  • alpha-carbon
  • beta-monooxygenase
  • klinman
The taxonomic range for the selected organisms is: Homo sapiens
The enzyme appears in selected viruses and cellular organisms
Synonyms
alpha-hydroxyglycine amidating dealkylase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
alpha-hydroxyglycine amidating dealkylase
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-
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lyase, peptidyl-alpha hydroxyglycine
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-
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PAL
277052
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peptidyl-alpha-hydroxyglycine alpha-amidating lyase
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-
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peptidylamidoglycolate lyase
277052
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
amidine-lyase reaction
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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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SUBSTRATE
PRODUCT                       
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
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-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
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
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-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
Cu2+
activates
Mn2+
activates, wild-type
Ni2+
activates
Zn2+
activates, binding of Co2+ or Cd2+ to empty zinc-binding sites on PAL
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
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
diethyl dicarbonate
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Phenylglyoxal
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0215 - 0.0887
N-2,4,6-trinitrophenyl-D-Tyr-L-Val-(S)-alpha-hydroxy-Gly
additional information
additional information
apparent second-order rate constants at different pHs
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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
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.53
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Sephacryl S-300 purification step
additional information
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
25 - 37
assay at
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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SwissProt
Manually annotated by BRENDA team
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
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in A- and B-cells
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
Sequence
AMD_HUMAN
973
1
108332
Swiss-Prot
PURIFICATION/commentary
ORGANISM
UNIPROT
LITERATURE
CLONED/commentary
ORGANISM
UNIPROT
LITERATURE
expression in chinese hamster ovary K-1 cells
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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)
Manually annotated by BRENDA team
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