Literature summary for 1.4.3.13 extracted from

Duff, A.P.; Cohen, A.E.; Ellis, P.J.; Kuchar, J.A.; Langley, D.B.; Shepard, E.M.; Dooley, D.M.; Freeman, H.C.; Guss, J.M.
The crystal structure of Pichia pastoris lysyl oxidase (2003), Biochemistry, 42, 15148-15157.

Search for more literature for 1.4.3.13

Crystallization (Commentary)

Crystallization (Comment)	Organism
purified recombinant enzyme, X-ray structure determination and analysis at 1.65 A resolution, modelling	Komagataella pastoris

Metals/Ions

Metals/Ions	Comment	Organism	Structure
copper	enzyme is a copper amino axidase, contains 1 type II copper atom per subunit	Komagataella pastoris

Natural Substrates/ Products (Substrates)

Natural Substrates	Organism	Comment (Nat. Sub.)	Natural Products	Comment (Nat. Pro.)	Rev.	Reac.
peptidyl-L-lysyl-peptide + O2 + H2O	Komagataella pastoris	-	peptidyl-allysyl-peptide + NH3 + H2O2	-	?

Organism

Organism	UniProt	Comment	Textmining
Komagataella pastoris	-	-	-

Reaction

Reaction	Comment	Organism	Reaction ID
[protein]-L-lysine + O2 + H2O = [protein]-(S)-2-amino-6-oxohexanoate + NH3 + H2O2	active site structure, a unique funnel defines substrate specificity	Komagataella pastoris	a

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
peptidyl-L-lysyl-peptide + O2 + H2O	-	Komagataella pastoris	peptidyl-allysyl-peptide + NH3 + H2O2	-	?
tropoelastin + O2 + H2O	oxidation of L-lysine residues, substrate from mammalia	Komagataella pastoris	? + H2O2 + NH3	-	?

Subunits

Subunits	Comment	Organism
dimer	homodimer, subunit interface structure, overview	Komagataella pastoris
More	the enzymes' tertiary and quarternary fold is similar but the active site structure is more exposed and accesible compared to the structure of other quinone-containing copper amine oxidases	Komagataella pastoris

Synonyms

Synonyms	Comment	Organism
lysyl oxidase	-	Komagataella pastoris
PPLO	-	Komagataella pastoris

Cofactor

Cofactor	Comment	Organism	Structure
topaquinone	i.e. TPQ or 2,4,5-trihydroxyphenylalanine quinone, formed by posttranslational modification of a tyrosine residue	Komagataella pastoris

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Release 2023.1 (January 2023)