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Information on EC 4.99.1.10 - magnesium dechelatase
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EC Tree
4.99.1.10 magnesium dechelataseIUBMB Comments
Inhibited by Ca2+, Mg2+ and especially Hg2+. SGR has very low activity with chlorophyllide a and none with chlorophyll b. It acts on chlorophyll a both in its free form and in protein complex. SGRL, on the other hand, is more active with chlorophyllide a than with chlorophyll a. The magnesium formed is scavenged by MCS (metal-chelating substance).
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Word Map
- 4.99.1.10
- chlorophyllase
-
stay-green
- pheophytins
- pheophorbide
-
brassica
-
postharvest
-
light-harvesting
-
florets
-
non-yellowing
- broccoli
-
photosystem
-
shelf-life
-
cherry-oat
- diuraphis
-
mordvilko
-
health-promoting
- sulforaphane
-
uninfested
- glutamyl-trna
-
dephytylation
- aphid
-
rhopalosiphum
-
chlorophyll-binding
-
aphid-infested
- noxia
- glucosinolate
The enzyme appears in viruses and cellular organisms
Reaction Schemes
+
2
=
+
+
2
=
+
Synonyms
mg-dechelatase, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
MCS
MDS
Mg-dechelatase
SGR
SGRL
Mg-dechelatase
-
-
-
-
SGRL
-
-
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
chlorophyll a + 2 H+ = pheophytin a + Mg2+
(1)
-
-
-
chlorophyllide a + 2 H+ = pheophorbide a + Mg2+
(2)
-
-
-
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PATHWAY SOURCE
PATHWAYS
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SYSTEMATIC NAME
IUBMB Comments
chlorophyll a magnesium lyase
Inhibited by Ca2+, Mg2+ and especially Hg2+. SGR has very low activity with chlorophyllide a and none with chlorophyll b. It acts on chlorophyll a both in its free form and in protein complex. SGRL, on the other hand, is more active with chlorophyllide a than with chlorophyll a. The magnesium formed is scavenged by MCS (metal-chelating substance).
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
chlorophyll a + 2 H+
pheophytin a + Mg2+
-
recombinant SGR1/2 extracts Mg from chlorophyll a but has very low or no activity against chlorophyllide a, while isoform SGRL has higher dechelating activity against chlorophyllide a compared to chlorophyll a
-
-
?
chlorophyllide a + 2 H+
pheophorbide a + Mg2+
-
recombinant SGR1/2 extracts Mg from chlorophyll a but has very low or no activity against chlorophyllide a, while isoform SGRL has higher dechelating activity against chlorophyllide a compared to chlorophyll a
-
-
?
additional information
?
-
-
the enzyme is not active with chlorophyllide a
-
-
?
additional information
?
-
-
the enzyme exhibits no activity against chlorophyll b and chlorophyllide a, protochlorophyll am chlorophyll c2, and Zn-chlorophyll a
-
-
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
chlorophyll a + 2 H+
pheophytin a + Mg2+
-
recombinant SGR1/2 extracts Mg from chlorophyll a but has very low or no activity against chlorophyllide a, while isoform SGRL has higher dechelating activity against chlorophyllide a compared to chlorophyll a
-
-
?
chlorophyllide a + 2 H+
pheophorbide a + Mg2+
-
recombinant SGR1/2 extracts Mg from chlorophyll a but has very low or no activity against chlorophyllide a, while isoform SGRL has higher dechelating activity against chlorophyllide a compared to chlorophyll a
-
-
?
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Anemia, Hypochromic
In vitro enzymatic chlorophyll catabolism in wheat elicited by cereal aphid feeding.
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.000081
chlorophyllin a
-
in 50 mM Tris-tricine buffer, at 37°C and pH 8.8
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
50
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
physiological function
physiological function
-
the activity of Mg-dechelatase is closely associated with the chlorophyll degradation during the leaf senescence process in harvested Chinese flowering cabbages under dark conditions
physiological function
-
the enzyme plays an important role in the process of autumnal coloring of the foliage by catalyzing the first step of chlorophyll degradation
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UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). SGR1_ARATH
268
0
30052
Swiss-Prot
Chloroplast (Reliability: 1)
SGR2_ARATH
271
0
30753
Swiss-Prot
Chloroplast (Reliability: 2)
SGRL_ARATH
260
0
29892
Swiss-Prot
Chloroplast (Reliability: 5)
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
100
-
at high ionic strength, the enzyme extract is inactivated after 10 min at 100°C
55
-
the purified protein is relatively heat stable and loses half of its activity after 10 min at 55°C
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
ammonium sulfate precipitation, DEAE-650M column chromatography, butyl-650M column chromatography, HW-55F gel filtration, and Sephacryl S-200 gel filtration
-
DEAE -Toyopearl column chromatography, butyl column chromatography. and HW-55 gel filtration
-
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli Rosetta (DE3) cells and in Arabidopsis thaliana cells
-
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
during dark-induced senescence, the activity increases over time until reaching a maximum at day 4, and then decreases
-
during strawberry fruit ripening, the Mg-dechelatase activity decreases from small green to large green stage and then increases again in mature fruit
-
Mg-dechelatase activity is higher in Diuraphis noxia-infested wheat lines than in uninfested plants
-
overall patterns of Mg-dechelatase activities display an increasing trend during the senescence process
-
the activity of M g-dechelatase in yellow leaves is higher than in green leaves
-
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Kaewsuksaeng, S.; Yamauchi, N.; Funamoto, Y.; Aiamla-Or, S.; Shigyo, M.; Kanlayanarat, S.
Partially purification of Mg-dechelatase in relation to chlorophyll degradation in broccoli (Brassica oleracea L. Italica group) florets
Acta Hortic.
875
509-514
2010
Brassica oleracea
-
brenda
Buechert, A.; Civello, P.; Martinez, G.
Characterization of Mg-dechelating substance in senescent and pre-senescent Arabidopsis thaliana leaves
Biol. Plant.
55
75-82
2011
Arabidopsis thaliana
-
brenda
Kraj, W.
Chlorophyll degradation and the activity of chlorophyllase and Mg-dechelatase during leaf senescence in Fagus sylvatica
Dendrobiology
74
43-57
2015
Fagus sylvatica
-
brenda
Yang, R.; Wang, J.; Nie, X.; Zhuang, Y.; Gu, Z.; Guo, Q.
Chlorophyll degradation and lignification of fresh-cut water fennel treated with a complex chemical solution and subsequent packaging
Food Sci. Biotechnol.
25
483-488
2016
Oenanthe javanica
-
brenda
Wang, T.; Quisenberry, S.S.; Ni, X.; Tolmay, V.
Enzymatic chlorophyll degradation in wheat near-isogenic lines elicited by cereal aphid (Homoptera Aphididae) feeding
J. Econ. Entomol.
97
661-667
2004
Triticum aestivum
brenda
Zhang, X.; Zhang, Z.; Li, J.; Wu, L.; Guo, J.; Ouyang, L.; Xia, Y.; Huang, X.; Pang, X.
Correlation of leaf senescence and gene expression/activities of chlorophyll degradation enzymes in harvested Chinese flowering cabbage (Brassica rapa var. parachinensis)
J. Plant Physiol.
168
2081-2087
2011
Brassica rapa
brenda
Suzuki, T.; Shioi, Y.
Re-examination of Mg-dechelation reaction in the degradation of chlorophylls using chlorophyllin a as a substrate
Photosynth. Res.
74
217-223
2002
Chenopodium album
brenda
Shimoda, Y.; Ito, H.; Tanaka, A.
Arabidopsis STAY-GREEN, Mendels green cotyledon gene, encodes magnesium-dechelatase
Plant Cell
28
2147-2160
2016
Arabidopsis thaliana
brenda
Matsuda, K.; Shimoda, Y.; Tanaka, A.; Ito, H.
Chlorophyll a is a favorable substrate for Chlamydomonas Mg-dechelatase encoded by STAY-GREEN
Plant Physiol. Biochem.
109
365-373
2016
Chlamydomonas reinhardtii
brenda
Costa, M.; Civello, P.; Chaves, A.; Martnez, G.
Characterization of Mg-dechelatase activity obtained from Fragaria x ananassa fruit
Plant Physiol. Biochem.
40
111-118
2002
Fragaria x ananassa
-
brenda
Suzuki, T.; Kunieda, T.; Murai, F.; Morioka, S.; Shioi, Y.
Mg-dechelation activity in radish cotyledons with artificial and native substrates, Mg-chlorophyllin a and chlorophyllide a
Plant Physiol. Biochem.
43
459-464
2005
Raphanus sativus
brenda
Kunieda, T.; Amano, T.; Shioi, Y.
Search for chlorophyll degradation enzyme, Mg-dechelatase, from extracts of Chenopodium album with native and artificial substrates
Plant Sci.
169
177-183
2005
Chenopodium album
-
brenda
Shi, J.; Gao, L.; Zuo, J.; Wang, Q.; Wang, Q.; Fan, L.
Exogenous sodium nitroprusside treatment of broccoli florets extends shelf life, enhances antioxidant enzyme activity, and inhibits chlorophyll-degradation
Postharvest Biol. Technol.
116
98-104
2016
Brassica oleracea
-
brenda
Tang, L.; Okazawa, A.; Fukusaki, E.; Kobayashi, A.
Removal of magnesium by Mg-dechelatase is a major step in the chlorophyll-degrading pathway in Ginkgo biloba in the process of autumnal tints
Z. Naturforsch. C
55
923-926
2001
Ginkgo biloba
brenda
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