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Information on EC 6.6.1.1 - magnesium chelatase and Organism(s) Pisum sativum and UniProt Accession O22437

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EC Tree
     6 Ligases
         6.6 Forming nitrogen—metal bonds
             6.6.1 Forming coordination complexes
                6.6.1.1 magnesium chelatase
IUBMB Comments
This is the first committed step of chlorophyll biosynthesis and is a branchpoint of two major routes in the tetrapyrrole pathway.
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This record set is specific for:
Pisum sativum
UNIPROT: O22437
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The taxonomic range for the selected organisms is: Pisum sativum
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Synonyms
magnesium chelatase, mg-chelatase, mg chelatase, chli1, xantha-f, abar/chlh, magnesium-chelatase, mg-chelatase h, chelatase h subunit, chli protein, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
magnesium-chelatase
-
-
-
-
magnesium-protoporphyrin chelatase
-
-
-
-
magnesium-protoporphyrin IX chelatase
-
-
-
-
Mg-chelatase
Mg-protoporphyrin IX magnesio-lyase
-
-
-
-
protoporphyrin IX magnesium-chelatase
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-
-
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protoporphyrin IX Mg-chelatase
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-
-
-
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
ATP + protoporphyrin IX + Mg2+ + H2O = ADP + phosphate + Mg-protoporphyrin IX + 2 H+
show the reaction diagram
this is the first committed step of chlorophyll biosynthesis and is a branchpoint of two major routes in the tetrapyrrole pathway
ATP + protoporphyrin IX + Mg2+ + H2O = ADP + phosphate + Mg-protoporphyrin IX + 2 H+
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Ligation
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
Mg-protoporphyrin IX magnesium-lyase
This is the first committed step of chlorophyll biosynthesis and is a branchpoint of two major routes in the tetrapyrrole pathway.
CAS REGISTRY NUMBER
COMMENTARY hide
9074-88-8
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
ATP + protoporphyrin IX + Mg2+ + H2O
ADP + phosphate + Mg-protoporphyrin IX + H+
show the reaction diagram
-
-
?
ATP + protoporphyrin IX + Mg2+ + H2O
ADP + phosphate + Mg-protoporphyrin IX + H+
show the reaction diagram
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
ATP + protoporphyrin IX + Mg2+ + H2O
ADP + phosphate + Mg-protoporphyrin IX + H+
show the reaction diagram
-
-
?
ATP + protoporphyrin IX + Mg2+ + H2O
ADP + phosphate + Mg-protoporphyrin IX + H+
show the reaction diagram
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Mg2+
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required
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
N-ethylmaleimide
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potent, IC50 of 0.02 mM
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
ATP
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required for activation and chelation steps
GENOMES UNCOUPLED 4
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GUN4 enhances measureable Mg-protoporphyrin IX in chloroplast extracts
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IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.02
N-ethylmaleimide
Pisum sativum
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potent, IC50 of 0.02 mM
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.000002
-
activity in chloroplast extracts
0.0000024
-
pellet of broken fractionated chloroplasts
0.0000026
-
supernatant of broken fractionated chloroplasts
0.00002
-
broken unfractionated chloroplasts
0.0001
-
intact chloroplasts
additional information
-
3fold to 4fold higher values than in cucumber chloroplasts
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
Uniprot
Manually annotated by BRENDA team
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
additional information
-
multicomponent enzyme, requires at least two proteins, one membrane-associated and one soluble
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Manually annotated by BRENDA team
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
CHLD_PEA
754
0
82865
Swiss-Prot
Chloroplast (Reliability: 3)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
150000
-
subunit H ChlH, SDS-PAGE
44000
-
subunit I ChlI, SDS-PAGE
93000
-
subunit D ChlD, SDS-PAGE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
26% loss of activity in chloroplasts subjected to hypotonic lysis and freeze-thaw cycles
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Walker, C.J.; Weinstein, J.D.
In vitro assay of the chlorophyll biosynthetic enzyme Mg-chelatase: resolution of the activity into soluble and membrane-bound fractions
Proc. Natl. Acad. Sci. USA
88
5789-5793
1991
Cucumis sativus, Pisum sativum
Manually annotated by BRENDA team
Walker, C.J.; Willows, R.D.
Mechanism and regulation of Mg-chelatase
Biochem. J.
327
321-333
1997
Arabidopsis thaliana, Cucumis sativus, Hordeum vulgare, Pisum sativum, Rhodobacter capsulatus, Cereibacter sphaeroides, Synechocystis sp. (P51634)
Manually annotated by BRENDA team
Luo, M.; Weinstein, J.D.; Walker, C.J.
Magnesium chelatase subunit D from pea: characterization of the cDNA, heterologous expression of an enzymatically active protein and immunoassay of the native protein
Plant Mol. Biol.
41
721-731
1999
Pisum sativum (O22437), Pisum sativum
Manually annotated by BRENDA team
Adhikari, N.D.; Orler, R.; Chory, J.; Froehlich, J.E.; Larkin, R.M.
Porphyrins promote the association of GENOMES UNCOUPLED 4 and a Mg-chelatase subunit with chloroplast membranes
J. Biol. Chem.
284
24783-24796
2009
Arabidopsis thaliana, Pisum sativum
Manually annotated by BRENDA team