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Information on EC 4.1.2.10 - (R)-mandelonitrile lyase and Organism(s) Prunus serotina and UniProt Accession P52706

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EC Tree
     4 Lyases
         4.1 Carbon-carbon lyases
             4.1.2 Aldehyde-lyases
                4.1.2.10 (R)-mandelonitrile lyase
IUBMB Comments
A variety of enzymes from different sources and with different properties. Some are flavoproteins, others are not. Active towards a number of aromatic and aliphatic hydroxynitriles (cyanohydrins).
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This record set is specific for:
Prunus serotina
UNIPROT: P52706
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Word Map
The taxonomic range for the selected organisms is: Prunus serotina
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
Synonyms
mandelonitrile lyase, athnl, (r)-oxynitrilase, (r)-(+)-mandelonitrile lyase, pahnl5, aphnl, r-selective hnl, pahnl1, ejhnl, acix9_0562, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
(R)-(+)-Mandelonitrile lyase
-
(R)-(+)-Mandelonitrile lyase
-
-
-
-
(R)-Mandelonitrile lyase
-
-
-
-
(R)-Oxynitrilase
-
-
-
-
D-alpha-hydroxynitrile lyase
-
-
-
-
D-Hydroxynitrile lyase
-
-
-
-
D-Oxynitrilase
-
-
-
-
Hydroxynitrile lyase
-
-
-
-
Lyase, mandelonitrile
-
-
-
-
MDL
-
-
-
-
Oxynitrilase
-
-
-
-
PhaMDL
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
cyanohydrin formation
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
(R)-mandelonitrile benzaldehyde-lyase (cyanide-forming)
A variety of enzymes from different sources and with different properties. Some are flavoproteins, others are not. Active towards a number of aromatic and aliphatic hydroxynitriles (cyanohydrins).
CAS REGISTRY NUMBER
COMMENTARY hide
9024-43-5
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
(R)-mandelonitrile
cyanide + benzaldehyde
show the reaction diagram
in Prunus serotina Ehrh. macerates, the cyanogenic diglucoside (R)-amygdalin undergoes stepwise degradation to HCN catalyzed by amygdalin hydrolase, prunasin hydrolase, and (R)-(+)-mandelonitrile lyase
-
-
?
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
(R)-mandelonitrile
cyanide + benzaldehyde
show the reaction diagram
in Prunus serotina Ehrh. macerates, the cyanogenic diglucoside (R)-amygdalin undergoes stepwise degradation to HCN catalyzed by amygdalin hydrolase, prunasin hydrolase, and (R)-(+)-mandelonitrile lyase
-
-
?
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
Ehrh.
UniProt
Manually annotated by BRENDA team
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
temporal expression of amygdalin hydrolase and (R)-(+)-mandelonitrile lyase in ripening fruit. Expression may be under transcriptional control during fruit maturation. (R)-(+)-mandelonitrile lyase transcripts are localized within cotyledonary parenchyma cell
Manually annotated by BRENDA team
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
MDL1_PRUSE
563
0
61200
Swiss-Prot
Secretory Pathway (Reliability: 1)
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Zheng, L.; Poulton, J.E.
Temporal and spatial expression of amygdalin hydrolase and (R)-(+)-mandelonitrile lyase in black cherry seeds
Plant Physiol.
109
31-39
1995
Prunus serotina (P52706), Prunus serotina
Manually annotated by BRENDA team