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BRENDA support

Literature summary for 1.4.3.2 extracted from

  • Rey-Suarez, P.; Acosta, C.; Torres, U.; Saldarriaga-Cordoba, M.; Lomonte, B.; Nunez, V.
    MipLAAO, a new L-amino acid oxidase from the redtail coral snake Micrurus mipartitus (2018), PeerJ, 6, e4924 .
    View publication on PubMedView publication on EuropePMC

Organism

Organism UniProt Comment Textmining
Micrurus mipartitus A0A2U8QPE6 mRNA transcripts show six isoforms with minor variations among them
-

Posttranslational Modification

Posttranslational Modification Comment Organism
glycoprotein presence of three putative N-glycosylation sites Micrurus mipartitus

Source Tissue

Source Tissue Comment Organism Textmining
venom
-
Micrurus mipartitus
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Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
L-leucine + H2O + O2
-
Micrurus mipartitus 4-methyl-2-oxopentanoate + NH3 + H2O2
-
?
L-tryptophan + H2O + O2
-
Micrurus mipartitus 3-(1H-indol-3-yl)-2-oxopropanoate + NH3 + H2O2
-
?
L-tyrosine + H2O + O2
-
Micrurus mipartitus 3-(4-hydroxyphenyl)-2-oxopropanoate + NH3 + H2O2
-
?
additional information enzyme shows a preference for hydrophobic amino acids Micrurus mipartitus ?
-
-

Subunits

Subunits Comment Organism
? x * 59101, MALDI-TOF Micrurus mipartitus

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
8
-
-
Micrurus mipartitus

pI Value

Organism Comment pI Value Maximum pI Value
Micrurus mipartitus calculated from sequence
-
8.9

General Information

General Information Comment Organism
evolution enzyme is placed within the clade of homologous proteins from elapid snakes, characterized by the conserved serine at position 223 Micrurus mipartitus