Reference to 1.2.3.1; Id = 740764 - BRENDA Enzyme Database

Crystallization (Commentary)

Crystallization (Comment)	Organism
molecular modeling. The structures of the isoforms Aox1 to Aox4 are highly preserved and even more conserved than their amino acid sequences. The binding site is composed by a highly conserved region of the Mo center and ligands, and by residues Gln722, Lys889, Arg917 and Ser1085 (mAOX3 numbering), and by a region, which is different among the several isoforms and is located just above the conserved region. The binding site conserved region is also composed by Phe919 (mAOX3 numbering) and by at least one or two hydrophobic residues containing aromatic rings in their side chains (His, Tyr and Phe)	Mus musculus
molecular modeling. The structures of the isoforms Aox1 to Aox4 are highly preserved and even more conserved than their amino acid sequences. The binding site is composed by a highly conserved region of the Mo center and ligands, and by residues Gln722, Lys889, Arg917 and Ser1085 (mAOX3 numbering), and by a region, which is different among the several isoforms and is located just above the conserved region. The binding site conserved region is also composed by Phe919 (mAOX3 numbering) and by at least one or two hydrophobic residues containing aromatic rings in their side chains (His, Tyr and Phe). The mAOX1 isoform has the wider specificity region with a variety of polar and charged amino acids	Mus musculus

Crystallization (Comment)

Organism

molecular modeling. The structures of the isoforms Aox1 to Aox4 are highly preserved and even more conserved than their amino acid sequences. The binding site is composed by a highly conserved region of the Mo center and ligands, and by residues Gln722, Lys889, Arg917 and Ser1085 (mAOX3 numbering), and by a region, which is different among the several isoforms and is located just above the conserved region. The binding site conserved region is also composed by Phe919 (mAOX3 numbering) and by at least one or two hydrophobic residues containing aromatic rings in their side chains (His, Tyr and Phe)

Mus musculus

molecular modeling. The structures of the isoforms Aox1 to Aox4 are highly preserved and even more conserved than their amino acid sequences. The binding site is composed by a highly conserved region of the Mo center and ligands, and by residues Gln722, Lys889, Arg917 and Ser1085 (mAOX3 numbering), and by a region, which is different among the several isoforms and is located just above the conserved region. The binding site conserved region is also composed by Phe919 (mAOX3 numbering) and by at least one or two hydrophobic residues containing aromatic rings in their side chains (His, Tyr and Phe). The mAOX1 isoform has the wider specificity region with a variety of polar and charged amino acids

Mus musculus

Organism

Organism	UniProt	Comment	Textmining
Mus musculus	Q148T8	-	-
Mus musculus	Q5SGK3	-	-
Mus musculus	Q8R387	-	-
Mus musculus	Q8VI15	-	-

Synonyms

Synonyms	Comment	Organism
AOX1	-	Mus musculus
AOX2	-	Mus musculus

Literature summary for 1.2.3.1 extracted from

Crystallization (Commentary)

Organism

Synonyms