Information on EC 3.1.1.14 - chlorophyllase

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The expected taxonomic range for this enzyme is: Eukaryota

EC NUMBER
COMMENTARY hide
3.1.1.14
-
RECOMMENDED NAME
GeneOntology No.
chlorophyllase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
chlorophyll + H2O = phytol + chlorophyllide
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis
hydrolysis of carboxylic ester
transesterification
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Biosynthesis of secondary metabolites
-
-
chlorophyll a degradation I
-
-
chlorophyll a degradation II
-
-
chlorophyll a degradation III
-
-
Metabolic pathways
-
-
Porphyrin and chlorophyll metabolism
-
-
SYSTEMATIC NAME
IUBMB Comments
chlorophyll chlorophyllidohydrolase
Chlorophyllase has been found in higher plants, diatoms, and in the green algae Chlorella [3]. This enzyme forms part of the chlorophyll degradation pathway and is thought to take part in de-greening processes such as fruit ripening, leaf senescence and flowering, as well as in the turnover and homeostasis of chlorophyll [4]. This enzyme acts preferentially on chlorophyll a but will also accept chlorophyll b and pheophytins as substrates [5]. Ethylene and methyl jasmonate, which are known to accelerate senescence in many species, can enhance the activity of the hormone-inducible form of this enzyme [5].
CAS REGISTRY NUMBER
COMMENTARY hide
9025-96-1
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
-
-
Manually annotated by BRENDA team
var. saccharifera
-
-
Manually annotated by BRENDA team
cv. Agridulce
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
SwissProt
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
chlorophyllase enzyme activity in the peel of ripe fruit is about 2.8fold higher than in unripe fruit suggesting that it may play a role in degreening of fruit; Var. Dasheheri
-
-
Manually annotated by BRENDA team
L. China tree
-
-
Manually annotated by BRENDA team
Musa cavendishii
Cavendish banana
-
-
Manually annotated by BRENDA team
3 varieties: Hojiblance, Picual, and Arbequina
-
-
Manually annotated by BRENDA team
female and male landraces
-
-
Manually annotated by BRENDA team
sour cherry
-
-
Manually annotated by BRENDA team
European plum
-
-
Manually annotated by BRENDA team
bird cherry
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
-
type II chlorophyllase takes part in chlorophyll degradation in stored broccoli florets
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
13-OH-chlorophyll a + H2O
phytol + 13-OH-chlorophyllide a
show the reaction diagram
-
in varieties Hojiblanca and Picual
-
?
4-nitrophenyl butyrate + H2O
4-nitrophenol + butyrate
show the reaction diagram
-
-
-
-
?
4-nitrophenyl decanoate + H2O
4-nitrophenol + decanoate
show the reaction diagram
-
-
-
-
?
bacteriochlorophyll + H2O
?
show the reaction diagram
bacteriochlorophyll + H2o
bacteriochlorophyllide + phytol
show the reaction diagram
-
-
-
-
?
bacteriochlorophyll a + H2O
bacteriochlorophyllide a + phytol
show the reaction diagram
-
-
-
?
bacteriochlorophyll a + Triton X-100 + H2O
bacteriochlorophyllide a tritonyl ester
show the reaction diagram
-
-
-
?
chlorobium chlorophyll + H2O
?
show the reaction diagram
-
-
-
-
ir
chlorophyll + H2O
chlorophyllide + ?
show the reaction diagram
chlorophyll + H2O
chlorophyllide + phytol
show the reaction diagram
chlorophyll + H2O
phytol + chlorophyllide
show the reaction diagram
chlorophyll a + CH3OH + phytol
methylchlorophyllide + ?
show the reaction diagram
-
-
-
-
chlorophyll a + H2O
?
show the reaction diagram
-
-
-
?
chlorophyll a + H2O
chlorophyllide a + phytol
show the reaction diagram
chlorophyll a + H2O
phytol + chlorophyllide
show the reaction diagram
chlorophyll a + H2O
phytol + chlorophyllide a
show the reaction diagram
chlorophyll a + Triton X-100 + H2O
tritonyl ester of chlorophyllide a tritonyl ester
show the reaction diagram
-
-
-
-
chlorophyll a/b + H2O
phytol + chlorophyllide
show the reaction diagram
chlorophyll aXXX ester + alcohol
chlorophyllide a(alcohol) + phytol
show the reaction diagram
-
-
-
?
chlorophyll b + H2O
?
show the reaction diagram
-
-
-
?
chlorophyll b + H2O
chlorophyllide b + phytol
show the reaction diagram
chlorophyll b + H2O
phytol + chlorophyllide
show the reaction diagram
-
stereospecific for the substrate, no activity with the C13-epimer
-
?
chlorophyll b + H2O
phytol + chlorophyllide b
show the reaction diagram
chlorophyllide a + phytol
chlorophyll a + H2O
show the reaction diagram
-
-
-
r
p-nitrophenyl butyrate + H2O
p-nitrophenol + butyrate
show the reaction diagram
-
-
-
-
?
p-nitrophenyl decanoate + H2O
p-nitrophenol + decanoate
show the reaction diagram
-
-
-
-
?
p-nitrophenyl palmitate + H2O
p-nitrophenol + palmitate
show the reaction diagram
-
-
-
-
?
pheophorbide a methyl ester + H2O
?
show the reaction diagram
-
-
-
?
pheophytin + H2O
?
show the reaction diagram
-
-
-
-
?
pheophytin + H2O
pheophorbide + ?
show the reaction diagram
-
-
-
-
?
pheophytin + H2O
phytol + pheophorbide
show the reaction diagram
-
-
-
?
pheophytin a + H2O
?
show the reaction diagram
-
-
-
-
ir
pheophytin a + H2O
pheophorbide a + phytol
show the reaction diagram
-
-
-
-
?
pheophytin a + H2O
phytol + pheophorbide
show the reaction diagram
pheophytin b + H2O
?
show the reaction diagram
-
-
-
-
ir
pheophytin b + H2O
? + phytol
show the reaction diagram
-
-
-
-
?
pheophytin b + H2O
phytol + pheophorbide
show the reaction diagram
-
-
-
?
pyrobacteriochlorophyll a + Triton X-100 + H2O
pyrobacteriochlorophyllide a tritonyl ester
show the reaction diagram
-
-
-
?
pyrochlorophyll a + Triton X-100 + H2O
pyrochlorophyllide a tritonyl ester + phytol
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
13-OH-chlorophyll a + H2O
phytol + 13-OH-chlorophyllide a
show the reaction diagram
-
in varieties Hojiblanca and Picual
-
?
chlorophyll + H2O
chlorophyllide + phytol
show the reaction diagram
-
-
-
-
ir
chlorophyll + H2O
phytol + chlorophyllide
show the reaction diagram
chlorophyll a + H2O
phytol + chlorophyllide a
show the reaction diagram
chlorophyll a/b + H2O
phytol + chlorophyllide
show the reaction diagram
chlorophyll b + H2O
phytol + chlorophyllide b
show the reaction diagram
pheophytin a + H2O
phytol + pheophorbide
show the reaction diagram
-
in varieties Hojiblanca and Picual
-
?
additional information
?
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
-
divalent cations stimulate
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
4-hydroxymercuribenzoate
acetone
activates at lower concentration, Chlase2 reaches its maximal activity in 40% acetone, in 40-60% acetone the activity is reduced, overview
beta-carotene
-
in absence of other lipids, inhibits chlorophyl a conversion
canola oil
-
presence of 10%, 20%, and 30% of canola oil decreased the activity of entrapped chlorophyllase by 60%, 75%, and 80%, respectively
-
concanavalin A
-
-
-
diethyldicarbonate
diisopropyl fluorophosphate
Eupergit C
-
immobilization support
-
Eupergit C/EDA
-
immobilization support
-
iodoacetamide
levulinic acid
-
inhibits the chlorophyll synthesis in greening leaves, alters the chlorophyll a/chlorophyll b ratio
N-ethylmaleimide
NaF3(CN)6
-
2 mM, 17% inhibition
-
phenylmethanesulfonyl fluoride
-
-
phenylmethylsulfonyl fluoride
pheophytin b
-
substrate inhibition above 0.005 mM
phosphatidyl glycerol
-
and sulfoquinovosyldiacylglycerol, inactivation in a cooperative manner
phytol
PMSF
-
irreversible, 89.2% inhibition at 10 mM, 1 h preincubation at pH 7.0 and 30C
refined bleached deodorized canola oil
-
20%
-
sulfoquinovosyldiacylglycerol
-
and phosphatidyl glycerol, inactivation in a cooperative manner
Triton X-100
additional information
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2-mercaptoethanol
acetone
beta-carotene
-
increases hydrolytic activity
dithiothreitol
fulvic acid
-
0.125-0.5 mg/ml
humic acid
-
0.125-0.5 mg/ml
humin
-
0.125-0.5 mg/ml
-
L-alpha-phosphatidyl-DL-glycerol
-
increases hydrolytic activity
L-alpha-phosphatidylcholine
-
increases hydrolytic activity
lecithin
-
enhances hydrolysis of chlorophyll
Lipids
wounding
-
induces enzyme expression from gene ATHCOR1 in leaves
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.05 - 0.069
4-nitrophenyl decanoate
0.0334
bacteriochlorophyll
-
-
0.004
bacteriochlorophyll a
-
pH 7.5, 30C
0.006 - 69
Chlorophyll
0.002 - 0.466
chlorophyll a
0.003 - 0.652
chlorophyll b
570
p-nitrophenyl butyrate
-
final concentration of 10% v/v acetonitrile at 25C
0.52
p-nitrophenyl decanoate
-
final concentration of 10% v/v acetonitrile at 37C
0.2
p-nitrophenyl palmitate
-
final concentration of 10% v/v acetonitrile at 37C
0.0764 - 0.143
pheophorbide a methyl ester
0.000206 - 0.09
pheophytin
0.0027 - 0.015
pheophytin a
0.0055 - 0.0064
pheophytin b
additional information
additional information
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
8.05 - 9.43
4-nitrophenyl decanoate
566
Chlorophyll
Triticum aestivum
-
-
0.0024 - 0.072
chlorophyll a
0.0037 - 0.072
chlorophyll b
10.3
p-nitrophenyl butyrate
Triticum aestivum
-
-
0.52
p-nitrophenyl decanoate
Triticum aestivum
-
-
0.2
p-nitrophenyl palmitate
Triticum aestivum
-
-
0.0039 - 0.259
pheophorbide a methyl ester
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0078 - 0.1551
chlorophyll a
0.0119 - 0.1105
chlorophyll b
0.0272 - 3.397
pheophorbide a methyl ester
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.00072
-
etiolated leaf
0.074
mutant enzyme H247A, in 100 mM sodium phosphate, pH 7.4, at 40C
0.149
mutant enzyme H239A, in 100mM sodium phosphate, pH 7.4, at 40C
0.15
-
unpurified homogenate, at pH 7.0 and 30C
0.372
mutant enzyme H66A, in 100 mM sodium phosphate, pH 7.4, at 40C
0.51
-
unpurified homogenate, at pH 7.0 and 30C
0.52
mutant enzyme H226A, in 100mM sodium phosphate, pH 7.4, at 40C
0.68
-
unpurified homogenate, at pH 7.0 and 30C
3.68
-
free enzyme, at pH 6.0 and 40C
5.53
-
after 3.73fold purification, isoform Chlase F1, at pH 7.0 and 30C
7.42
-
after 3.73fold purification, isoform Chlase F2, at pH 7.0 and 30C
7.43
wild type isoform CLH2, in 100 mM sodium phosphate, pH 7.4, at 40C
8.52
-
enzyme immobilized in alginate, at pH 6.0 and 40C
9.52
-
after 18.67fold purification, isoform Chlase F2, at pH 7.0 and 30C
9.79
-
enzyme isolated at the exponential growth phase
10.9
-
enzyme immobilized in magnetic iron oxide nanoparticles-alginate, at pH 6.0 and 40C
14.75
-
after 28.92fold purification, isoform Chlase F1, at pH 7.0 and 30C
15
-
21 chlorophyllide a at 25C, 10 chlorophyllide b at 25C
16.92
-
after 24.88fold purification, isoform Chlase F2, at pH 7.0 and 30C
19.47
-
after 28.63fold purification, isoform Chlase F1, at pH 7.0 and 30C
35.55
-
etioplast
41.3
-
chloroplast
134.4
-
enzyme isolated at the stationary growth phase
322
-
optimization of chlorophyllase-catalyzed hydrolysis of chlorophyll in monophasic organic solvent media, the catalytic efficiency of chlorophyllase in the undiluted organic solvent mixture is lower than that in the aqueous medium, overview
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6 - 7.5
-
hydrolysis of bacteriochlorophyll a
6 - 8
-
-
6.6 - 7.6
-
chlorophyll b, chlorophyllase type 1 and type 2
6.6 - 8.6
-
hydrolysis of chlorophyll a, chlorophyllase type 1 and type 2
7 - 8.5
-
hydrolysis of chlorophyll a
7
-
assay at, substrate chlorophyll
7.5 - 8
-
soluble enzyme
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.2 - 8.1
-
50% of maximal activity at pH 6.2 and 8.1
6.4 - 8.7
-
pH 6.4: about 70% of maximal activity, pH 8.7: about 80% of maximal activity, soluble enzyme
7 - 11.5
-
35% of maximal activity at pH 7.0, 60& of maximal activity at pH 11.5
7.5 - 8.8
-
pH 7.5: about 35% of maximal activity, pH 8.8: about 65% of maximal activity
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
20 - 30
-
-
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0 - 45
-
0C: about 35% of maximal activity, 45C: about 50% of maximal activity
30 - 70
-
-
30 - 50
-
-
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.7
-
calculation from sequence of cDNA
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
additional information
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
additional information
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
26000
-
gel filtration
33000
-
mature enzyme, SDS-PAGE
33800
-
calculated molecular weight
33880
-
calculation from sequence of cDNA
35000
-
precursor enzyme, SDS-PAGE
37110
-
calculated from amino acid sequence
39000
-
gel filtration
110000
-
gel filtration
130000
-
gel filtration
158000
-
gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dimer
-
2 * 65000, SDS-PAGE
tetramer
-
4 * 27000, SDS-PAGE
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
no modification
side-chain modification
additional information
the mature form is N-terminally processed after amino acids 21, 20 or 19
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
3
-
rapid inactivation
80737
5 - 8
isoform CLH1
715221
6 - 9
isozyme AtCLH2
681243
6 - 8
-
0C, loss of 2% of activity per day
80737
6 - 9
-
4C, 24 h, stable
80731
7.5
-
stable in presence or absence of 30% acetone
80731
8 - 10
isoform CLH2 shows about 80% of activity at pH 9.0 and is stable between pH 8.0 and 10.0
715221
8
-
stability decreases significantly above or below pH 8.0
665784
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4
-
24 h exposure at 4C followed by 10 d of recovery, leads to overall reduced enzyme activity with the eti5 mutant plants being more sensitive, during the stress time and the first day of recovery the enzyme activity is highly reduced, the enzyme activity is more affected during the experiment time in wild-type plants, overview
20
-
24 h, 30-50% loss of activity
30
-
not stable above a 10% concentration of acetone
35 - 50
-
enzyme half-life in the neat organic solvent compared to that in the aqueous medium in the first environment at temperature ranging from 35 to 50C is increased by 5.0 to 15.0 times, overview
38
-
24 h exposure at 4C followed by 10 d of recovery, leads to overall reduced enzyme activity with the eti5 mutant plants being more sensitive, during the stress time and the first day of recovery the enzyme activity is highly reduced, the enzyme activity is more affected during the experiment time in wild-type plants, overview
40
-
stable for 1 h
45
-
1 h, pH 7, citrate buffer, stable. Complete loss of activity in presence of 40% acetone
50
-
degradation after 40 min, more rapid at higher temperatures
65
-
destroyed within 10 min
additional information
-
association of chlorophyllase with mixed monogalactosyldiacylglycerol and phosphatidylglycerol and also with mixed digalactosyldiacylglycerol and phosphatidylglycerol leads to highly increased heat stability. Single lipids are shown to have a much lower or no stabilizing influence. Only with phosphatidylglycerol, in the absence of Mg2+, is any notable enzyme stabilization observed
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
60% loss of activity after dialysis against distilled water in the cold for 48 h
-
stabilized by chlorophyll
-
ORGANIC SOLVENT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Acetone
-
strong reduction of activity at above 40%
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20C, stable for at least 1 year without loss of activity
-
-80C, 25 mM Tris buffer, pH 8.0, 100 mM NaCl
-
25C, loss of 50% activity within 6 days
-
4C, loss of 50% within 18 days
-
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
2 isoenzymes: type 1 chlorophyllase and type 2 chlorophyllase
-
ammonium sulfate precipitation and Sephadex G-200gel filtration
amylose resin affinity column chromatography and DEAE Sepharose column chromatography; amylose resin affinity column chromatography and DEAE Sepharose column chromatography; amylose resin affinity column chromatography and DEAE Sepharose column chromatography
cold acetone extraction and column chromatography
-
Ni2+-NTA column chromatography
-
no isoenzymes
-
partial
partially
-
protein-A agarose bead immunoprecipitation
-
recombinant enzymes in the membrane fraction from Nicotiana tabacum chloroplasts by ultracentrifugation
recombinant His6-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography, or by using a microtiter plate purification method with immobilization of the enzyme, overview
-
recombinant isozyme AtCLH2 from Escherichia coli strain BL21 (DE3)
recombinant maltose-binding fusion protein from Escherichia coli
-
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Chlase gene, DNA and amino acid sequence determination and anaylsis, expression of precursor full-length wild-type Chlase and of a mutant ChlaseDELTAN lacking the N-terminal 21 amino acids, which corresponds to the mature enzyme, in two heterologous plant systems: in Cucurbita pepo cv. Maayan plants using a ZYMV-based viral vector infective clone system and inoculation of cotyledons, and transiently in Nicotiana tabacum cv. Samsun NN chloroplast membranes of protoplasts, expression of full-length and truncated enzyme versions as thioredoxin fusion proteins in Escherichia coli
expressed in Escherichia coli
expressed in Escherichia coli BL21 (DE3) cells
-
expressed in Escherichia coli BL21 cells
-
expressed in Escherichia coli BL21(DE3) cells; expressed in Escherichia coli BL21(DE3) cells
expressed in Escherichia coli Rosseta-Gami B (DE3) cells; expressed in Escherichia coli Rosseta-Gami B (DE3) cells; expressed in Escherichia coli Rosseta-Gami B (DE3) cells
expressed in Escherichia coli; expressed in Escherichia coli strain BL21(DE3)
-
expression as His6-tagged enzyme in Escherichia coli strain BL21(DE3)
-
expression in Escherichia coli
expression of antisense construct of gene CLH3 in broccoli plants using Agrobacterium tumefaciens-mediated transformation; expression of antisense constructs of gene CLH1 in broccoli plants using Agrobacterium tumefaciens-mediated transformation; expression of antisense constructs of gene CLH2 in broccoli plants using Agrobacterium tumefaciens-mediated transformation
expression of gene ATHCOR1 in Escherichia coli BL21 as maltose-binding protein fusion protein, cloning of the gene into an expression vector for transformation of Arabidopsis thaliana plants
-
expression of wild-type and mutant enzymes in Escherichia coli
-
gene chl1, DNA and amino acid sequence determination and anaylsis, transient expression of isozyme AtCLH1 as GFP-tagged protein, e.g. in senescent mesophyll protoplasts, expression analysis; gene chl2, DNA and amino acid sequence determination and anaylsis, transient expression of isozyme AtCLH2 as GFP-tagged protein, e.g. in senescent mesophyll protoplasts, expression analysis
gene chl2, expression anaylsis, recombinant expression in Escherichia coli strain BL21 (DE3)
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
chlorophyllase type I is suppressed in UV-B treated broccoli on day 4
-
expression pattern of isoform CLH2 shows an expression increase in senescent tissue and is higher in stem tissue than in inflorescences; isoform CLH1 shows a higher expression in presenescent tissue compared to senescent tissue and stem
in the case of isoform CLH1, an important decrease in expression is observed after day 0, since an over 50fold drop is found from day 0 to day 3 of control florets after hormone-treatment (100ppm 6-benzylaminopurine)
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
D170A
inactive; inactive
H226A
the mutation causes almost complete loss of Chlase activity; the mutation causes almost complete loss of Chlase activity
H239A
the mutation causes almost complete loss of Chlase activity; the mutation causes almost complete loss of Chlase activity
H247A
the mutation causes almost complete loss of Chlase activity; the mutation causes almost complete loss of Chlase activity
H66A
the mutation causes almost complete loss of Chlase activity; the mutation causes almost complete loss of Chlase activity
S141A
inactive; inactive
C234A
-
site-directed mutagenesis, highly reduced activity compared to the wild-type enzyme
C248A
-
site-directed mutagenesis, highly reduced activity compared to the wild-type enzyme
C282A
-
site-directed mutagenesis, highly reduced activity compared to the wild-type enzyme
D191N
-
site-directed mutagenesis, inactive mutant
D264N
-
site-directed mutagenesis, highly reduced activity compared to the wild-type enzyme
H100A
-
site-directed mutagenesis, highly reduced activity compared to the wild-type enzyme
H161A
-
site-directed mutagenesis, inactive mutant
H241A
-
site-directed mutagenesis, about 90% reduced activity compared to the wild-type enzyme
H254A
-
site-directed mutagenesis, nearly inactive mutant
H254Y
-
site-directed mutagenesis, about 90% reduced activity compared to the wild-type enzyme
H262A
-
site-directed mutagenesis, nearly inactive mutant
H262Y
-
site-directed mutagenesis, nearly inactive mutant
H81A
-
site-directed mutagenesis, about 85% reduced activity compared to the wild-type enzyme
S162A
-
site-directed mutagenesis, nearly inactive mutant
S167A
-
site-directed mutagenesis, about 50% reduced activity compared to the wild-type enzyme
additional information
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
agriculture
biotechnology
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encapsulation of the enzyme in micelles of different media within alginate hydrogels increases the enzyme activity in e.g. Tris buffer or hexane, extent of enhancement of the partition coefficient depends on the amount and hydrophobicity of the components intrduced into alginate, affecting the hydrophobic-hydrophilic balance of the gel
synthesis
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useful tool for preparing chlorophyllides and chlorophyll derivatives esterified with various alcohols