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Information on EC 3.1.1.14 - chlorophyllase and Organism(s) Arabidopsis thaliana and UniProt Accession Q9M7I7

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EC Tree
     3 Hydrolases
         3.1 Acting on ester bonds
             3.1.1 Carboxylic-ester hydrolases
                3.1.1.14 chlorophyllase
IUBMB Comments
Chlorophyllase has been found in higher plants, diatoms, and in the green algae Chlorella . 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 . This enzyme acts preferentially on chlorophyll a but will also accept chlorophyll b and pheophytins as substrates . 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 .
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Arabidopsis thaliana
UNIPROT: Q9M7I7
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Word Map
The taxonomic range for the selected organisms is: Arabidopsis thaliana
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
Synonyms
chlorophyllase, chlase, atclh1, boclh1, atclh2, crclh1, chlorophyllase 1, cyanoclh, chlorophyllase1, caclh, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
chlorophyllase-2
-
Chlase
chlorophyll chlorophyllido-hydrolyase
-
-
-
-
chlorophyll-chlorophyllido hydrolase
-
coronatine-induced protein
-
-
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
chlorophyll + H2O = phytol + chlorophyllide
show the reaction diagram
also catalyzes chlorophyllide transfer, e.g. converts chlorophyll to methylchlorophyllide
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of carboxylic ester
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
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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
chlorophyll + H2O
phytol + chlorophyllide
show the reaction diagram
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
additional information
?
-
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
chlorophyll + H2O
phytol + chlorophyllide
show the reaction diagram
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
-
the enzyme is involved in the regulation of chlorophyll a and b content
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
-
divalent cations stimulate
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
acetone
activates at lower concentration, Chlase2 reaches its maximal activity in 40% acetone, in 40-60% acetone the activity is reduced, overview
Triton X-100
-
strong inhibition at 0.2-1.0%
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
acetone
activates at lower concentration, Chlase2 reaches its maximal activity in 40% acetone, in 40-60% acetone the activity is reduced, overview
wounding
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induces enzyme expression from gene ATHCOR1 in leaves
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.44
sequence calculation
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
-
developing, constitutive expression of gene AtChl2 and gene ATHCOR1, expression of recmbinant enzyme in mutant transgenic plants
Manually annotated by BRENDA team
additional information
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
CLH is located in the endoplasmic reticulum and the tonoplast of intact plant cells
Manually annotated by BRENDA team
CLH is located in the endoplasmic reticulum and the tonoplast of intact plant cells
-
Manually annotated by BRENDA team
additional information
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
chlorophyll breakdown is indistinguishable between wild-type plants and clh1 and clh1/clh2 mutant plants. By contrast, chlorophyll degradation is significantly delayed in an Arabidopsis thaliana mutant that lacks pheophytinase (PPH), catalyzing the breakdown of phytol and known to be associated with chlorophyll catabolism. These data indicate that PPH, not CLH1, is responsible for the majority of methyl jasmonate-enhanced chlorophyll breakdown, even though CLH1 is highly induced by methyl jasmonate
physiological function
CLH2 represents the minority of detectable CLH activity in Arabidopsis thaliana
malfunction
chlorophyll breakdown is indistinguishable between wild-type plants and clh1 and clh1/clh2 mutant plants. By contrast, chlorophyll degradation is significantly delayed in an Arabidopsis thaliana mutant that lacks pheophytinase (PPH), catalyzing the breakdown of phytol and known to be associated with chlorophyll catabolism. These data indicate that PPH, not CLH1, is responsible for the majority of MeJA-enhanced chlorophyll breakdown, even though CLH1 is highly induced by methyl jasmonate
physiological function
additional information
bioinformatics evaluation of plant chlorophyllases, overview
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
CLH2_ARATH
318
0
34904
Swiss-Prot
Chloroplast (Reliability: 4)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
35000
x * 35000, recombinant AtCLH2, SDS-PAGE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
x * 35000, recombinant AtCLH2, SDS-PAGE
?
x * 34850, sequence calculation
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
no glycoprotein
-
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6 - 9
isozyme AtCLH2
681243
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
38
-
24 h exposure at 4°C 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
4
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24 h exposure at 4°C 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
ORGANIC SOLVENT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Acetone
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strong reduction of activity at above 40%
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
4°C, stable
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant isozyme AtCLH2 from Escherichia coli strain BL21 (DE3)
recombinant maltose-binding fusion protein from Escherichia coli
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
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 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
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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 clh1, recombinant expression of YFP-tagged enzyme in Arabidopsis thaliana, the YFP-tagged enzyme is detected outside of chloroplasts in leaf protoplasts prepared from plants constitutively expressing CLH1-YFP
gene CLH1, sequence analysis, comparisons, and phylogenetic analysis, overview. Expression as insoluble protein
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
the enzyme is induced by estradiol and methyl jasmonate
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Todorov, D.T.; Karanov, E.N.; Smith, A.R.; Hall, M.A.
Chlorophyllase activity and chlorophyll content in wild type and eti5 mutant of Arabidopsis thaliana subjected to low and high temperatures
Biol. Plant.
46
633-636
2003
Arabidopsis thaliana
-
Manually annotated by BRENDA team
Benedetti, C.E.; Arruda, P.
Altering the expression of the chlorophyllase gene ATHCOR1 in transgenic Arabidopsis caused changes in the chlorophyll-to-chlorophyllide ratio
Plant Physiol.
128
1255-1263
2002
Arabidopsis thaliana
Manually annotated by BRENDA team
Kariola, T.; Brader, G.; Li, J.; Palva, E.T.
Chlorophyllase 1, a damage control enzyme, affects the balance between defense pathways in plants
Plant Cell
17
282-294
2005
Arabidopsis thaliana (O22527), Arabidopsis thaliana
Manually annotated by BRENDA team
Schenk, N.; Schelbert, S.; Kanwischer, M.; Goldschmidt, E.E.; Doermann, P.; Hoertensteiner, S.
The chlorophyllases AtCLH1 and AtCLH2 are not essential for senescence-related chlorophyll breakdown in Arabidopsis thaliana
FEBS Lett.
581
5517-5525
2007
Arabidopsis thaliana (O22527), Arabidopsis thaliana (Q9M7I7), Arabidopsis thaliana
Manually annotated by BRENDA team
Liao, Y.; An, K.; Zhou, X.; Chen, W.; Kuai, B.
AtCLH2, a typical but possibly distinctive chlorophyllase gene in Arabidopsis
J. Integr. Plant Biol.
49
531-539
2007
Arabidopsis thaliana (Q9M7I7)
-
Manually annotated by BRENDA team
Nowak, P.M.; Wozniakiewicz, M.; Michalik, M.; Fiedor, L.; Koscielniak, P.
Capillary coating as an important factor in optimization of the off-line and on-line MEKC assays of the highly hydrophobic enzyme chlorophyllase
Anal. Bioanal. Chem.
409
1493-1501
2017
Arabidopsis thaliana
Manually annotated by BRENDA team
Sharafi, E.; Dehestani, A.; Farmani, J.; Parizi, A.
Bioinformatics evaluation of plant chlorophyllase, the key enzyme in chlorophyll degradation
Appl. Food Biotechnol.
4
167-178
2017
Aegilops tauschii (N1R2K4), Amborella trichopoda (W1NV63), Arabidopsis lyrata subsp. lyrata (D7KI46), Arabidopsis thaliana (O22527), Beta vulgaris (A0A0J8FQE7), Brassica napus (A0A078ILD2), Brassica oleracea (Q8GTM3), Chenopodium album (Q9LE89), Citrus limon (B6DX58), Citrus sinensis (Q9MV14), Citrus unshiu (Q94LX1), Cucumis sativus (A0A0A0LNT6), Elaeis guineensis (XP_010934773), Ginkgo biloba (Q7Y0K5), Jatropha curcas (A0A067KVU1), Malus domestica (XP_008355440), Medicago truncatula (A0A072VHG0), Oryza sativa Japonica Group (Q7XEJ4), Pachira macrocarpa (C1JZ62), Phoenix dactylifera, Picea sitchensis (C0PR35), Picrorhiza kurrooa (A0A024CJ54), Piper betle (Q7XJ36), Populus trichocarpa (B9HUR3), Prunus mume (XP_008235366), Pyrus x bretschneideri (G3K720), Sesamum indicum, Setaria italica (K4AC16), Solanum lycopersicum (XP_010326690), Solanum pennellii (F1BPW6), Solanum tuberosum (M1A7S9), Triticum aestivum (W6EIP8), Triticum urartu (M8AD49), Vitis vinifera (F6HI77), Zea mays (B4FAJ2)
-
Manually annotated by BRENDA team
Hu, X.; Makita, S.; Schelbert, S.; Sano, S.; Ochiai, M.; Tsuchiya, T.; Hasegawa, S.F.; Hoertensteiner, S.; Tanaka, A.; Tanaka, R.
Reexamination of chlorophyllase function implies its involvement in defense against chewing herbivores
Plant Physiol.
167
660-670
2015
Arabidopsis thaliana (O22527), Arabidopsis thaliana (Q9M7I7), Arabidopsis thaliana Col-0 (O22527), Arabidopsis thaliana Col-0 (Q9M7I7)
Manually annotated by BRENDA team