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Literature summary for 1.4.3.21 extracted from

  • Moore, R.H.; Spies, M.A.; Culpepper, M.B.; Murakawa, T.; Hirota, S.; Okajima, T.; Tanizawa, K.; Mure, M.
    Trapping of a dopaquinone intermediate in the TPQ cofactor biogenesis in a copper-containing amine oxidase from Arthrobacter globiformis (2007), J. Am. Chem. Soc., 129, 11524-11534.
    View publication on PubMed
Search for more literature for 1.4.3.21

Crystallization (Commentary)

Crystallization (Comment) Organism
the X-ray crystal structure of D298K at 1.7 A resolution Arthrobacter globiformis

Protein Variants

Protein Variants Comment Organism
D298K in contrast to M602K and wild-type enzyme, the quinone in D298K does not react with any of the hydrazines. D298K shows no activity toward oxidative deamination of 2-phenylethylamine. The quinone formed in D298K is trapped in a conformation that can not react with amines. D298K contains a quinone other than topaquinone Arthrobacter globiformis
M602K the mutant enzyme shows 20% activity toward 2-phenylethylamine in comparison to wild-type enzyme Arthrobacter globiformis

Metals/Ions

Metals/Ions Comment Organism Structure
copper
-
 Arthrobacter globiformis

Organism

Organism UniProt Comment Textmining
Arthrobacter globiformis P46881
-
-

Purification (Commentary)

Purification (Comment) Organism
-
 Arthrobacter globiformis

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2-phenylethylamine + H2O + O2
-
 Arthrobacter globiformis 2-phenylethanal + NH3 + H2O2
-
 ?

Synonyms

Synonyms Comment Organism
AGAO
-
 Arthrobacter globiformis
CAO
-
 Arthrobacter globiformis
Copper amine oxidase
-
 Arthrobacter globiformis

Cofactor

Cofactor Comment Organism Structure
topaquinone
-
 Arthrobacter globiformis