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
4.3.2.5
-
RECOMMENDED NAME
GeneOntology No.
peptidylamidoglycolate lyase
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
peptidylamidoglycolate = peptidyl amide + glyoxylate
show the reaction diagram
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
amidine-lyase reaction
-
-
-
-
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.
SYNONYMS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
alpha-hydroxyglycine amidating dealkylase
-
-
-
-
lyase, peptidyl-alpha hydroxyglycine
-
-
-
-
peptidyl-alpha-hydroxyglycine alpha-amidating lyase
-
-
-
-
CAS REGISTRY NUMBER
COMMENTARY
131689-50-4
-
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
SwissProt
Manually annotated by BRENDA team
EC 1.14.17.3 (PHM) and EC 4.3.2.5 (PAL) are part of a bifunctional protein
-
-
Manually annotated by BRENDA team
Mus musculus C57BL/6J
-
-
-
Manually annotated by BRENDA team
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
-
-
Manually annotated by BRENDA team
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
-
-
Manually annotated by BRENDA team
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
-
-
Manually annotated by BRENDA team
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
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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
Mus musculus C57BL/6J
-
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
-
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
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-hydroxyglycine-extended peptide
peptidyl amide + glyoxylate
show the reaction diagram
-
-
-
-
-
alpha-hydroxyglycine-extended peptide
peptidyl amide + glyoxylate
show the reaction diagram
-
-
-
-
?
alpha-hydroxyglycine-extended peptide
peptidyl amide + glyoxylate
show the reaction diagram
-
-
-
?
alpha-hydroxyglycine-extended peptide
peptidyl amide + glyoxylate
show the reaction diagram
-
-
-
?
alpha-hydroxyglycine-extended peptide
peptidyl amide + glyoxylate
show the reaction diagram
-
the alpha-hydroxyglycine moiety produced by EC 1.14.17.3 is of the S configuration
-
-
?
alpha-N-acetyl-Tyr-Val-alpha-hydroxyglycine
alpha-N-acetyl-Tyr-Val-NH2 + glyoxylate
show the reaction diagram
Q9V5E1, Q9W1L5
-
-
-
?
alpha-N-acetyl-Tyr-Val-alpha-hydroxyglycine
alpha-N-acetyl-Tyr-Val-NH2 + glyoxylate
show the reaction diagram
P14925
-
-
-
?
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
-
-
-
?
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
-
-
-
-
-
Nalpha-acetyl-Tyr-Val-alpha-hydroxyglycine
Nalpha-acetyl-Tyr-Val-NH2 + glyoxylate
show the reaction diagram
-
-
-
-
?
Nalpha-acetyl-Tyr-Val-alpha-hydroxyglycine
Nalpha-acetyl-Tyr-Val-NH2 + 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
-
-
-
-
?
peptidylamidoglycolate
peptidyl amide + glyoxylate
show the reaction diagram
Q9V5E1, Q9W1L5
-
-
-
?
peptidylamidoglycolate
peptidyl amide + glyoxylate
show the reaction diagram
P14925
-
-
-
?
peptidylamidoglycolate
peptidyl amide + glyoxylate
show the reaction diagram
Mus musculus C57BL/6J
-
-
-
-
?
trinitrophenyl-D-Tyr-L-Val-alpha-hydroxy-Gly
trinitrophenyl-D-Tyr-L-Val-NH2 + 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
-
-
-
?
dansyl-Tyr-Val-alpha-hydroxyglycine
dansyl-Tyr-Val-NH2 + glyoxylate
show the reaction diagram
-
-
-
?
additional information
?
-
Mus musculus, Mus musculus C57BL/6J
-
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
-
-
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
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
-
-
-
-
?
peptidylamidoglycolate
peptidyl amide + glyoxylate
show the reaction diagram
Q9V5E1, Q9W1L5
-
-
-
?
peptidylamidoglycolate
peptidyl amide + glyoxylate
show the reaction diagram
P14925
-
-
-
?
peptidylamidoglycolate
peptidyl amide + glyoxylate
show the reaction diagram
Mus musculus C57BL/6J
-
-
-
-
?
additional information
?
-
Mus musculus, Mus musculus C57BL/6J
-
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
-
-
-
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
-
no cofactor requirement
-
additional information
-
no cofactor requirement
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Cd2+
Q9V5E1, Q9W1L5
activates the enzyme; activates the enzyme
Cd2+
P14925
activates the enzyme
Cd2+
P19021
activates, binding of Co2+ or Cd2+ to empty zinc-binding sites on PAL
Co2+
Q9V5E1, Q9W1L5
activates the enzyme; activates the enzyme
Co2+
P14925
activates the enzyme
Co2+
P19021
activates, binding of Co2+ or Cd2+ to empty zinc-binding sites on PAL
Cu2+
P19021
activates
Ni2+
P19021
activates
Zn2+
-
0.7 mol per mol enzyme
Zn2+
P19021
activates, binding of Co2+ or Cd2+ to empty zinc-binding sites on PAL
Mn2+
P19021
activates, wild-type
additional information
P19021
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
LITERATURE
IMAGE
(R)-2-phenylbutyl-alpha-hydroxy-Gly
-
-
(S)-2-phenylbutyl-alpha-hydroxy-Gly
-
-
2-mercaptoethanol
-
-
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
diethyl dicarbonate
-
-
EDTA
-
divalent metals restore activity
EDTA
-
addition of 0.5-1 M reduces activity to 50%, Ca2+, Mn2+, Co2+ or Ni2+ restore activity
EDTA
Q9V5E1, Q9W1L5
1 mM; 1 mM
EGTA
-
addition of 0.5-1 M reduces activity to 50%, Ca2+, Mn2+, Co2+ or Ni2+ restore activity
HCl
-
0.5 M guanidinium HCl reduces activity to 28%
K2SO4
-
150 mM
NaCl
-
150 mM
o-phenanthroline
-
-
phenylacetyl-alpha-hydroxy-Gly
-
competitive inhibition
Phenylglyoxal
-
-
Urea
-
addition of 1 M urea reduces activity to 58%
KCl
-
150 mM
additional information
-
relatively resistant to thiol reagents and urea
-
additional information
-
-
-
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
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Cd2+
Q9V5E1, Q9W1L5
;
Cd2+
P14925
-
Co2+
Q9V5E1, Q9W1L5
;
Co2+
P14925
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
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
-
37C, pH 6.5
0.013
alpha-N-Acetyl-Tyr-Val-alpha-hydroxyglycine
P14925
-
0.045
alpha-N-Acetyl-Tyr-Val-alpha-hydroxyglycine
Q9V5E1, Q9W1L5
-
0.238
alpha-N-Acetyl-Tyr-Val-alpha-hydroxyglycine
Q9V5E1, Q9W1L5
-
0.035 - 0.048
Dansyl-Tyr-Val-alpha-hydroxyglycine
-
37C, pH 7.0
0.0215
N-2,4,6-trinitrophenyl-D-Tyr-L-Val-(S)-alpha-hydroxy-Gly
P19021
pH 6.0, 25C, wild-type enzyme
0.0887
N-2,4,6-trinitrophenyl-D-Tyr-L-Val-(S)-alpha-hydroxy-Gly
P19021
pH 6.0, 25C, metal-depleted enzyme
0.46
N-benzoyl-alpha-hydroxy-Gly
-
37C, pH 6.5
0.0102
Nalpha-Acetyl-Tyr-Val-alpha-hydroxyglycine
-
37C, pH 5.5, E707Q
0.0139
Nalpha-Acetyl-Tyr-Val-alpha-hydroxyglycine
-
37C, pH 5.5, recombinant wild-type
0.0156
Nalpha-Acetyl-Tyr-Val-alpha-hydroxyglycine
-
37C, pH 5.5, H690A
0.0214
Nalpha-Acetyl-Tyr-Val-alpha-hydroxyglycine
-
37C, pH 5.5, D705N
0.0231
Nalpha-Acetyl-Tyr-Val-alpha-hydroxyglycine
-
37C, pH 5.5, H585A
0.034
Nalpha-Acetyl-Tyr-Val-alpha-hydroxyglycine
-
37C, pH 7.4, with endoprotease Arg-C digested PAM-3 protein
0.037
Nalpha-Acetyl-Tyr-Val-alpha-hydroxyglycine
-
37C, pH 7.4, undigested PAM-3 protein
0.038
Nalpha-Acetyl-Tyr-Val-alpha-hydroxyglycine
-
37C, pH 7
0.0985
Nalpha-Acetyl-Tyr-Val-alpha-hydroxyglycine
-
37C, pH 5.5, H786A
0.33
Nalpha-Acetyl-Tyr-Val-alpha-hydroxyglycine
-
37C, pH 5.5
0.014
trinitrophenyl-D-Tyr-L-Val-alpha-hydroxy-Gly
-
37C, pH 6.6, PGL domain of transmembrane truncated enzyme: dAE
0.018
trinitrophenyl-D-Tyr-L-Val-alpha-hydroxy-Gly
-
37C, pH 6.6, PGL domain of full expressed enzyme: AE
0.019
trinitrophenyl-D-Tyr-L-Val-alpha-hydroxy-Gly
-
37C, pH 6.6, monofunctional lyase: PGL
0.027
trinitrophenyl-D-Tyr-L-Val-alpha-hydroxy-Gly
-
37C, pH 6.5
0.033
trinitrophenyl-D-Tyr-L-Val-alpha-hydroxy-Gly
-
37C, pH 6.6
0.0023 - 0.004
dansyl-Tyr-Val-Gly
-
37C, pH 6
additional information
additional information
P19021
apparent second-order rate constants at different pHs
-
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
P19021
pH 6.0, 25C, metal-depleted enzyme
25.7
N-2,4,6-trinitrophenyl-D-Tyr-L-Val-(S)-alpha-hydroxy-Gly
P19021
pH 6.0, 25C, wild-type enzyme
86
Nalpha-Acetyl-Tyr-Val-alpha-hydroxyglycine
-
37C, pH 7.4, with endoprotease Arg-C digested PAM-3 protein
92
Nalpha-Acetyl-Tyr-Val-alpha-hydroxyglycine
-
37C, pH 7.4, undigested PAM-3 protein
220
Nalpha-Acetyl-Tyr-Val-alpha-hydroxyglycine
-
37C, pH 7
380
Nalpha-Acetyl-Tyr-Val-alpha-hydroxyglycine
-
37C, pH 5.5
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
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
acetylmethionyl pyruvate
-
37C, pH 6.6, monofunctional lyase: PGL
4.8
acetylmethionyl pyruvate
-
37C, pH 6.6, PGL domain of full expressed enzyme: AE
0.049
acetylphenylalanyl pyruvate
-
37C, pH 6.6, monofunctional lyase: PGL
0.071
acetylphenylalanyl pyruvate
-
37C, pH 6.6, PGL domain of full expressed enzyme: AE
0.55
acetyltyrosyl pyruvate
-
37C, pH 6.6, monofunctional lyase: PGL
0.92
acetyltyrosyl pyruvate
-
37C, pH 6.6, PGL domain of full expressed enzyme: AE
0.77
phenylacetyl-alpha-hydroxy-Gly
-
37C, pH 6.5
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.25 - 0.32
-
dansyl-Tyr-Val-Gly as substrate
0.53
-
Sephacryl S-300 purification step
4.5 - 8.3
-
dansyl-Tyr-Val-alpha-hydroxyglycine as substrate
57.24
-
affinity chromatography step II
510
-
Mono Q pool A, after concentration
12000
-
Superose 12 pool
23000
-
PGL domain of full expressed enzyme: AE
76000
-
PGL domain of transmembrane truncated enzyme: dAE
180000
-
monofunctional lyase: PGL
16000000
-
Mono Q fraction
additional information
P19021
-
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5.5 - 7
P19021
-
6.5
Q9V5E1, Q9W1L5
-
7.5
Q9V5E1, Q9W1L5
-
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
25 - 37
P19021
assay at
37
-
assay at
37
-
assay at
37
-
assay at
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
Manually annotated by BRENDA team
Q9W1L5
ap-let neuron
Manually annotated by BRENDA team
-
in A-, B- and D-cells
Manually annotated by BRENDA team
-
in A- and B-cells
Manually annotated by BRENDA team
-
in peripheral islet and B-cells
Manually annotated by BRENDA team
Mus musculus C57BL/6J
-
-
-
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
additional information
-
secretory granular fraction
-
Manually annotated by BRENDA team
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
38000
-
gel filtration
648704
43900
Q9V5E1, Q9W1L5
monomer, secreted, rhodopsin-tagged protein, calculated from amino acid sequence
666112
44400
Q9V5E1, Q9W1L5
monomer, secreted, rhodopsin-tagged protein, calculated from amino acid sequence
666112
45000
-
gel filtration
648691
50000
-
PAL domain, conversion of the 50000 MW form into a 43000 MW form occurs during gel filtration
648697
53000
-
gel filtration
648701
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
438571
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
?
-
x * 41000, SDS-PAGE
?
Q9V5E1, Q9W1L5
x * 49300, rhodopsin-tagged protein, SDS-PAGE
?
Q9V5E1, Q9W1L5
x * 51300, rhodopsin-tagged protein, SDS-PAGE
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20C, 50% glycerol containing 1 mg/ml bovine serum albumin
-
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
enzyme is encoded by the intergranular domain of the PAM-encoding cDNA
-
expression in chinese hamster ovary K-1 cells
-
expression in a human embryonic kidney cell line that lacks regulated secretory granules
-
expression in Chinese hamster ovary cells
-
expression in cultured Sf9 insect cells
-
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
D590N
-
no secretion
D599N
-
no secretion
D652N
-
no secretion
D705N
-
much less secretion and less active than wild-type
E707Q
-
much less secretion than wild-type
H532A
-
no secretion
H585A
-
less active than wild-type
H603A
-
no secretion
H690A
-
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