Information on EC 1.3.1.75 - 3,8-divinyl protochlorophyllide a 8-vinyl-reductase (NADPH)

Word Map on EC 1.3.1.75
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Specify your search results
Select one or more organisms in this record:
Show additional data
Do not include text mining results
Include (text mining) results (more...)
Include results (AMENDA + additional results, but less precise; more...)


The expected taxonomic range for this enzyme is: Eukaryota, Bacteria

EC NUMBER
COMMENTARY hide
1.3.1.75
-
RECOMMENDED NAME
GeneOntology No.
3,8-divinyl protochlorophyllide a 8-vinyl-reductase (NADPH)
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
protochlorophyllide a + NADP+ = 3,8-divinyl protochlorophyllide a + NADPH + H+
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
oxidation
-
-
-
-
redox reaction
-
-
-
-
reduction
-
-
-
-
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
bacteriochlorophyll a biosynthesis
-
-
bacteriochlorophyll c biosynthesis
-
-
bacteriochlorophyll d biosynthesis
-
-
bacteriochlorophyll e biosynthesis
-
-
chlorophyll a biosynthesis I
-
-
chlorophyll a biosynthesis II
-
-
chlorophyll metabolism
-
-
Porphyrin and chlorophyll metabolism
-
-
Metabolic pathways
-
-
Biosynthesis of secondary metabolites
-
-
SYSTEMATIC NAME
IUBMB Comments
protochlorophyllide-a:NADP+ C-81-oxidoreductase
The enzyme, found in higher plants, green algae, and some phototrophic bacteria, is involved in the production of monovinyl versions of (bacterio)chlorophyll pigments from their divinyl precursors. It can also act on 3,8-divinyl chlorophyllide a. cf. EC 1.3.7.13, 3,8-divinyl protochlorophyllide a 8-vinyl-reductase (ferredoxin).
CAS REGISTRY NUMBER
COMMENTARY hide
143590-98-1
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
UniProt
Manually annotated by BRENDA team
rifampicin-resistant mutant strain J001 derived from wild-type strain 2.4.1, gene bchXYZ
-
-
Manually annotated by BRENDA team
rifampicin-resistant mutant strain J001 derived from wild-type strain 2.4.1, gene bchXYZ
-
-
Manually annotated by BRENDA team
a rifampicin-resistant variant of wild-type strain CGA009, gene bciB
-
-
Manually annotated by BRENDA team
a rifampicin-resistant variant of wild-type strain CGA009, gene bciB
-
-
Manually annotated by BRENDA team
light-inducible
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
metabolism
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
2,4-divinyl chlorophyllide a + NADPH + H+
2-vinyl-4-ethyl chlorophyllide a + NADP+
show the reaction diagram
chlorophyllide a + NADP+
divinyl chlorophyllide a + NADPH + H+
show the reaction diagram
divinyl chlorophyllide a + NADPH + H+
monovinyl chlorophyllide a + NADP+
show the reaction diagram
-
-
-
-
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
2,4-divinyl chlorophyllide a + NADPH + H+
2-vinyl-4-ethyl chlorophyllide a + NADP+
show the reaction diagram
chlorophyllide a + NADP+
divinyl chlorophyllide a + NADPH + H+
show the reaction diagram
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
NADP+
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.17
-
partially purified enzyme
additional information
-
assay development
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.5 - 8.5
-
about half-maximal activity at pH 5.5 and pH 8.5, no activity below pH 5.2 and above pH 11.0
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
25
-
assay at
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
10 - 50
-
about half-maximal activity at 10°C and 50°C
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
60
-
complete inactivation after 2 min
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
glycerol stabilizes the membrane-bound enzyme, it has no effect on the solubilized enzyme
-
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-80 °C, partially purified enzyme, stable for several months
-
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
partial
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
gene bchXYZa, cloning and DNA and amino acid sequence determination and analysis, the plasmid carrying genes bchXYZ is used for complementation fo bchXYZ-deficient mutant strains of Rhodobacter sphaeroides, Rhodobacter palustris, Chlorobium tepidum, and Rhodobacter castenholzii
-
recombinant protein expressed in Escherichia coli
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information