Any feedback?
Please rate this page
(enzyme.php)
(0/150)

BRENDA support

BRENDA Home
show all | hide all No of entries

Information on EC 4.1.99.3 - deoxyribodipyrimidine photo-lyase and Organism(s) Oryza sativa and UniProt Accession Q6F6A2

for references in articles please use BRENDA:EC4.1.99.3
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
     4 Lyases
         4.1 Carbon-carbon lyases
             4.1.99 Other carbon-carbon lyases
                4.1.99.3 deoxyribodipyrimidine photo-lyase
IUBMB Comments
A flavoprotein (FAD), containing a second chromophore group. The enzyme catalyses the reactivation by light of irradiated DNA. A similar reactivation of irradiated RNA is probably due to a separate enzyme.
Specify your search results
Select one or more organisms in this record: ?
This record set is specific for:
Oryza sativa
UNIPROT: Q6F6A2
Show additional data
Do not include text mining results
Include (text mining) results
Include results (AMENDA + additional results, but less precise)
Word Map
hide
The taxonomic range for the selected organisms is: Oryza sativa
The enzyme appears in selected viruses and cellular organisms
Synonyms
ssdna, primase, photolyase, dna photolyase, cryptochrome 1, cpd photolyase, cry-dash, cpd-photolyase, cryptochrome dash, cyclobutane pyrimidine dimer photolyase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
class II CPD photolyase
-
-
class II cyclobutane pyrimidine dimer photolyase
-
-
class II photolyase
-
-
CPD photolyase
-
-
CPDII
-
-
deoxyribodipyrimidine photolyase
-
-
-
-
deoxyribonucleate pyrimidine dimer lyase (photosensitive)
-
-
-
-
deoxyribonucleic cyclobutane dipyrimidine photolyase
-
-
-
-
deoxyribonucleic photolyase
-
-
-
-
dipyrimidine photolyase (photosensitive)
-
-
-
-
DNA cyclobutane dipyrimidine photolyase
-
-
-
-
DNA photolyase
-
-
-
-
DNA-photoreactivating enzyme
-
-
-
-
lyase, deoxyribonucleate pyrimidine dimer
-
-
-
-
photolyase
-
-
-
-
photoreactivating enzyme
-
-
-
-
phr A photolyase
-
-
-
-
PhrB photolyase
-
-
-
-
PRE
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
C-C-bond cleavage
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
deoxyribocyclobutadipyrimidine pyrimidine-lyase
A flavoprotein (FAD), containing a second chromophore group. The enzyme catalyses the reactivation by light of irradiated DNA. A similar reactivation of irradiated RNA is probably due to a separate enzyme.
CAS REGISTRY NUMBER
COMMENTARY hide
37290-70-3
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
cyclobutadipyrimidine in DNA
2 pyrimidine residues in DNA
show the reaction diagram
-
-
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
FAD
-
binds the flavin cofactor in a pocket that is conserved in terms of its electronic properties. W399-W378-W406 may function as potential electron donors to the flavin and are possible candidate tryptophans for light-induced electron transfer
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
-
transgenic rice plants bearing the CPD photolyase gene of the UV-resistant rice cultivar Sasanishiki in the sense orientation reveal up to 45.7fold higher CPD photolyase activities compared to wildtype are significantly more resistant to UVB-induced growth damage, and maintain significantly lower CPD levels in their leaves during growth under elevated UVB radiation. Rice plants bearing the CPD photolyase gene in the antisense orientation have little photolyase activity, are severely damaged by elevated UVB radiation, and maintain higher CPD levels in its leaves during growth under UVB radiation.
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.2
-
assay at
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
30
-
assay at
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
-
-
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
-
CPD photolyase functions in chloroplasts. Nuclei and chloroplasts have a relatively high proportion of the phosphorylated protein form
Manually annotated by BRENDA team
-
CPD photolyase functions in mitochondria. Mitochondria show a high proportion of non-phosphorylated CPD photolyase
Manually annotated by BRENDA team
-
CPD photolyase functions in nuclei. Nuclei and chloroplasts have a relatively high proportion of the phosphorylated protein form
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
-
the CPD photoreactivation rate is undetectable in chloroplasts, mitochondria or nuclei in transgenic rice (AS-D) engineered to express antisense RNA targeting CPD photolyase in wildtype Sasanishiki rice cultivar with low levels of CPD photolyase activity
metabolism
-
photoreduction kinetics of class II photolyases are very similar to those of the other classes with even higher photoreduction rates in class II as compared to class I. W399-W378-W406 electron-transfer pathway is conserved among class II CPD photolyase enzymes
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
54000
-
phosphorylated CPD photolyase. Nuclei and chloroplasts have a relatively high proportion of the phosphorylated form
56000
-
non-phosphorylated CPD photolyase. Mitochondria show a high proportion of non-phosphorylated CPD photolyase
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
phosphoprotein
-
-
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-70°C, 0.05 M sodium phosphate, pH 7.0, 0.1 M NaCl, 20% (v/v) glycerol
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
by using a Bio-Gel P6DG spin-column
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
GST-tagged class II CPD photolyase overexpressed in Escherichia coli
-
transgenic rice plants bearing the CPD photolyase gene of the UV-resistant rice cultivar Sasanishiki in the sense and antisense orientation are generated
-
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Hidema, J.; Taguchi, T.; Ono, T.; Teranishi, M.; Yamamoto, K.; Kumagai, T.
Increase in CPD photolyase activity functions effectively to prevent growth inhibition caused by UVB radiation
Plant J.
50
70-79
2007
Oryza sativa
Manually annotated by BRENDA team
Okafuji, A.; Biskup, T.; Hitomi, K.; Getzoff, E.D.; Kaiser, G.; Batschauer, A.; Bacher, A.; Hidema, J.; Teranishi, M.; Yamamoto, K.; Schleicher, E.; Weber, S.
Light-induced activation of class II cyclobutane pyrimidine dimer photolyases
DNA Repair
9
495-505
2010
Arabidopsis thaliana, Escherichia coli, Oryza sativa
Manually annotated by BRENDA team
Takahashi, M.; Teranishi, M.; Ishida, H.; Kawasaki, J.; Takeuchi, A.; Yamaya, T.; Watanabe, M.; Makino, A.; Hidema, J.
Cyclobutane pyrimidine dimer (CPD) photolyase repairs ultraviolet-B-induced CPDs in rice chloroplast and mitochondrial DNA
Plant J.
66
433-442
2011
Oryza sativa
Manually annotated by BRENDA team