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Information on EC 1.4.3.13 - protein-lysine 6-oxidase and Organism(s) Drosophila melanogaster

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EC Tree
     1 Oxidoreductases
         1.4 Acting on the CH-NH2 group of donors
             1.4.3 With oxygen as acceptor
                1.4.3.13 protein-lysine 6-oxidase
IUBMB Comments
Also acts on protein 5-hydroxylysine. This enzyme catalyses the final known enzymic step required for collagen and elastin cross-linking in the biosynthesis of normal mature extracellular matrices . These reactions play an important role for the development, elasticity and extensibility of connective tissue. The enzyme is also active on free amines, such as cadaverine or benzylamine [4,5]. Some isoforms can also use [protein]-N(6)-acetyl-L-lysine as substrate deacetamidating the substrate .
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This record set is specific for:
Drosophila melanogaster
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Word Map
The taxonomic range for the selected organisms is: Drosophila melanogaster
The expected taxonomic range for this enzyme is: Eukaryota, Archaea
Synonyms
lysyl oxidase, loxl2, loxl1, loxl4, loxl3, lox-pp, lysyl oxidases, lysyl oxidase-like 1, lysyl oxidase-like 2, lysyl oxidase-like, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
RAS excision protein
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
oxidation
-
-
-
-
oxidative deamination
-
-
-
-
redox reaction
-
-
-
-
reduction
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
protein-L-lysine:oxygen 6-oxidoreductase (deaminating)
Also acts on protein 5-hydroxylysine. This enzyme catalyses the final known enzymic step required for collagen and elastin cross-linking in the biosynthesis of normal mature extracellular matrices [4]. These reactions play an important role for the development, elasticity and extensibility of connective tissue. The enzyme is also active on free amines, such as cadaverine or benzylamine [4,5]. Some isoforms can also use [protein]-N(6)-acetyl-L-lysine as substrate deacetamidating the substrate [6].
CAS REGISTRY NUMBER
COMMENTARY hide
99676-44-5
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
agmatine + O2 + H2O
?
show the reaction diagram
-
-
-
?
cadaverine + O2 + H2O
?
show the reaction diagram
-
-
-
?
histamine + O2 + H2O
?
show the reaction diagram
-
-
-
?
lysine + O2 + H2O
?
show the reaction diagram
-
-
-
?
peptidyl-L-lysyl-peptide + O2 + H2O
peptidyl-allysyl-peptide + NH3 + H2O2
show the reaction diagram
-
-
-
?
putrescine + O2 + H2O
?
show the reaction diagram
-
-
-
?
spermidine + O2 + H2O
?
show the reaction diagram
-
-
-
?
spermine + O2 + H2O
?
show the reaction diagram
-
-
-
?
tropoelastin + O2 + H2O
?
show the reaction diagram
-
-
-
?
additional information
?
-
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
peptidyl-L-lysyl-peptide + O2 + H2O
peptidyl-allysyl-peptide + NH3 + H2O2
show the reaction diagram
-
-
-
?
additional information
?
-
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
lysyl tyrosylquinone
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
3-aminopropanenitrile
-
beta-aminopropionitrile
inhibition of LOXL-1
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
additional information
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
Q9V9X5_DROME
360
0
40833
TrEMBL
Secretory Pathway (Reliability: 2)
Q9W2C9_DROME
511
0
57908
TrEMBL
Secretory Pathway (Reliability: 2)
Q9N9Y8_DROME
511
0
57831
TrEMBL
Chloroplast (Reliability: 2)
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Molnar, J.; Fong, K.S.K.; He, Q.P.; Hayashi, K.; Kim, Y.; Fong, S.F.T.; Fogelgren, B.; Molnarne Szauter, K.; Mink, M.; Csiszar, K.
Structural and functional diversity of lysyl oxidase and the LOX-like proteins
Biochim. Biophys. Acta
1647
220-224
2003
Homo sapiens, Mus musculus, Drosophila melanogaster (Q9N9Y8), Drosophila melanogaster (Q9V9X5)
Manually annotated by BRENDA team
Bollinger, J.A.; Brown, D.E.; Dooley, D.M.
The Formation of lysine tyrosylquinone (LTQ) is a self-processing reaction. Expression and characterization of a Drosophila lysyl oxidase
Biochemistry
44
11708-11714
2005
Drosophila melanogaster (Q9V9X5)
Manually annotated by BRENDA team