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Information on EC 3.1.1.14 - chlorophyllase and Organism(s) Citrus sinensis and UniProt Accession Q9MV14

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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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Citrus sinensis
UNIPROT: Q9MV14
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The taxonomic range for the selected organisms is: Citrus sinensis
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
Synonyms
chlorophyllase, chlase, atclh1, boclh1, atclh2, crclh1, chlorophyllase 1, cyanoclh, caclh, chlase1, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Chlase
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chlorophyll chlorophyllido-hydrolyase
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of carboxylic ester
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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
Chlase is a rate-limiting enzyme in chlorophyll catabolism and is posttranslationally regulated, it catalyzes the cleavage of the hydrophobic thylakoid-anchoring phytol chain of chlorophyll from the porphyrin ring, resulting in the product chlorophyllide, which retains the typical green color, chlorophyll catabolic pathway, overview
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?
chlorophyll a + H2O
phytol + chlorophyllide
show the reaction diagram
chlorophyll a substrate from Petroselinum sativum leaves
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?
chlorophyll a + H2O
phytol + chlorophyllide a
show the reaction diagram
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?
additional information
?
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autolysis of chlorophyll appears to be brought about by enzymatic activity of chlorophyllase which upon membrane disruption and solubilization obtains access to its chlorophyll substrate
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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
chlorophyll + H2O
phytol + chlorophyllide
show the reaction diagram
Chlase is a rate-limiting enzyme in chlorophyll catabolism and is posttranslationally regulated, it catalyzes the cleavage of the hydrophobic thylakoid-anchoring phytol chain of chlorophyll from the porphyrin ring, resulting in the product chlorophyllide, which retains the typical green color, chlorophyll catabolic pathway, overview
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?
chlorophyll a + H2O
phytol + chlorophyllide a
show the reaction diagram
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?
additional information
?
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autolysis of chlorophyll appears to be brought about by enzymatic activity of chlorophyllase which upon membrane disruption and solubilization obtains access to its chlorophyll substrate
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?
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.06
sequence calculation
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
key enzyme in chlorophyll degradation
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?
CLH1_CITSI
329
0
35209
Swiss-Prot
Chloroplast (Reliability: 5)
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
x * 35250, sequence calculation
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
glycoprotein
the enzyme sequence contains 5 glycosylation sites at positions 77, 137, 229, 249, and 267
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
expression of full-length citrus Chlase results in limited chlorophyll breakdown in tobacco protoplasts and no visible leaf phenotype in whole plants, whereas expression of a Chlase version lacking the N-terminal 21 amino acids, i.e. ChlaseDELTAN, which corresponds to the mature protein, leads to extensive chlorophyll breakdown in both tobacco protoplasts and squash leaves, mutant ChlaseDELTAN-expressing squash leaves display a dramatic chlorotic phenotype in plants grown under low-intensity light, whereas under natural light a lesion-mimic phenotype occurrs, which follows the accumulation of chlorophyllide, a photodynamic chlorophyll breakdown product, phenotypes, overview
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant enzymes in the membrane fraction from Nicotiana tabacum chloroplasts by ultracentrifugation
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. Ma’ayan 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
gene Chlase1, sequence analysis, comparisons, and phylogenetic analysis, overview. Expression as insoluble protein
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Amir-Shapira, D.; Goldschmidt, E.E.; Altman, A.
Autolysis of chlorophyll in aqueous and detergent suspension of chloroplast fragments
Plant Sci.
43
201-206
1986
Citrus sinensis, Petroselinum crispum
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Manually annotated by BRENDA team
Harpaz-Saad, S.; Azoulay, T.; Arazi, T.; Ben-Yaakov, E.; Mett, A.; Shiboleth, Y.M.; Hoertensteiner, S.; Gidoni, D.; Gal-On, A.; Goldschmidt, E.E.; Eyal, Y.
Chlorophyllase is a rate-limiting enzyme in chlorophyll catabolism and is posttranslationally regulated
Plant Cell
19
1007-1022
2007
Citrus sinensis (Q9MV14)
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)
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Manually annotated by BRENDA team