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Literature summary for 1.4.3.2 extracted from

  • Georgieva, D.; Murakami, M.; Perband, M.; Arni, R.; Betzel, C.
    The structure of a native L-amino acid oxidase, the major component of the Vipera ammodytes ammodytes venomic, reveals dynamic active site and quaternary structure stabilization by divalent ions (2011), Mol. Biosyst., 7, 379-384.
    View publication on PubMed

Crystallization (Commentary)

Crystallization (Comment) Organism
purified native enzyme by sitting drop vapour diffusion method, using a protein concentration of 10 mg/ml, with 0.04 M zinc acetate and 16% w/v PEG 3350 as the precipitant, X-ray diffraction structure determination and analysis at 2.57 A resolution Vipera ammodytes ammodytes

Localization

Localization Comment Organism GeneOntology No. Textmining
extracellular
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Vipera ammodytes ammodytes
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Metals/Ions

Metals/Ions Comment Organism Structure
Zn2+ one Zn2+ ion is anchored to His75 at the beta-hairpin formed by the segment 73-86, which stabilizes the oligomeric state by bridging His75 and Glu279 of the adjacent protomer Vipera ammodytes ammodytes

Organism

Organism UniProt Comment Textmining
Vipera ammodytes ammodytes
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-
-

Posttranslational Modification

Posttranslational Modification Comment Organism
glycoprotein an N-acetylglucosamine group bound to the Asn172 side chain Vipera ammodytes ammodytes

Purification (Commentary)

Purification (Comment) Organism
native enzyme from venom by two repeated steps of anion exchange chromatography Vipera ammodytes ammodytes

Source Tissue

Source Tissue Comment Organism Textmining
venom
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Vipera ammodytes ammodytes
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Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information active site and substrate binding structure, overview Vipera ammodytes ammodytes ?
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?

Subunits

Subunits Comment Organism
More LAAO comprises the FAD-binding domain, the substrate binding domain, and the alpha-helical domain, the substrate binding domain is made up by residues 5-25, 73-129, 233-236 and 323-420, and contains 4 alpha-helices, formed by residues 16-25, 96-104, 375-383 and 386-401, and 11 beta-strands, residues 74-77, 82-85, 109-112, 120-123, 126-129, 233-236, 324-331, 345-347, 354-356, 367-374 and 412-419 Vipera ammodytes ammodytes

Synonyms

Synonyms Comment Organism
LAAO
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Vipera ammodytes ammodytes

Cofactor

Cofactor Comment Organism Structure
FAD the FAD-binding domain includes residues 35-72, 239-318 and 446-486. The secondary structure elements of this domain are 4 alpha-helices Vipera ammodytes ammodytes