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

BRENDA support

BRENDA Home
show all | hide all No of entries

Information on EC 2.1.1.160 - caffeine synthase and Organism(s) Camellia ptilophylla and UniProt Accession Q2HXI6

for references in articles please use BRENDA:EC2.1.1.160
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
     2 Transferases
         2.1 Transferring one-carbon groups
             2.1.1 Methyltransferases
                2.1.1.160 caffeine synthase
IUBMB Comments
Paraxanthine is the best substrate for this enzyme but the paraxanthine pathway is considered to be a minor pathway for caffeine biosynthesis [2,3].
Specify your search results
Select one or more organisms in this record: ?
This record set is specific for:
Camellia ptilophylla
UNIPROT: Q2HXI6
Show additional data
Do not include text mining results
Include (text mining) results
Include results (AMENDA + additional results, but less precise)
Word Map
The taxonomic range for the selected organisms is: Camellia ptilophylla
The enzyme appears in selected viruses and cellular organisms
Synonyms
caffeine synthase, tea caffeine synthase, tea caffeine synthase 1, 1-n-methyltransferase, n-1 methyltransferase, 7-n-methylxanthine methyltransferase, more
SYSTEMATIC NAME
IUBMB Comments
S-adenosyl-L-methionine:3,7-dimethylxanthine N1-methyltransferase
Paraxanthine is the best substrate for this enzyme but the paraxanthine pathway is considered to be a minor pathway for caffeine biosynthesis [2,3].
CAS REGISTRY NUMBER
COMMENTARY hide
155215-94-4
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
S-adenosyl-L-methionine + 1,7-dimethylxanthine
S-adenosyl-L-homocysteine + 1,3,7-trimethylxanthine
show the reaction diagram
additional information
?
-
substrate specificity, overview
-
-
?
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
S-adenosyl-L-methionine + 1,7-dimethylxanthine
S-adenosyl-L-homocysteine + 1,3,7-trimethylxanthine
show the reaction diagram
i.e. paraxanthine, alternative route in caffeine biosynthesis
i.e. caffeine
-
?
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
SwissProt
Manually annotated by BRENDA team
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
PCS1_CAMPL
365
0
40926
Swiss-Prot
-
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
construction and substrate specificity determination of chimeric mutant enzymes composed of theobromine synthase and inactive caffeine synthase, EC 2.1.1.160, overview
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
DNA and amino acid sequence determination and analysis, expression of wild-type and chimeric mutant enzymes in Escherichia coli strain BL21(DE3), phylogenetic analysis
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Yoneyama, N.; Morimoto, H.; Ye, C.X.; Ashihara, H.; Mizuno, K.; Kato, M.
Substrate specificity of N-methyltransferase involved in purine alkaloids synthesis is dependent upon one amino acid residue of the enzyme
Mol. Genet. Genomics
275
125-135
2006
Camellia irrawadiensis (Q2HXL9), Camellia ptilophylla (Q2HXI6), Theobroma cacao (Q2HXL8)
Manually annotated by BRENDA team