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1 Q biogenesis has been carried out on a yeast copper amine oxidase.
2 tion, which occurs in cofactor biogenesis in copper amine oxidases.
3 ning selective mechanism-based inhibitors of copper amine oxidases.
4 uinone nucleus found in the plasma and other copper amine oxidases.
5              The X-ray crystal structures of copper amine oxidase-1 from the yeast Hansenula polymorp
6  metabolism of a branched primary amine by a copper amine oxidase and suggests a novel type of revers
7 that resemble the ortho-quinone cofactors in copper amine oxidases and mediate the efficient and sele
8                                              Copper amine oxidases are a family of enzymes with quino
9 e N assimilation pathway: the replacement of copper amine oxidase by a flavin-dependent backup enzyme
10                          The expression of a copper amine oxidase (CAO) from Hansenula polymorpha in
11                                              Copper amine oxidase (CAO) is a dual-functioning enzyme
12 genesis of the topaquinone (TPQ) cofactor of copper amine oxidase (CAO) is self-catalyzed and require
13                                              Copper amine oxidases (CAOs) are responsible for the oxi
14                                          The copper amine oxidases (CAOs) catalyze both the single-tu
15                                          The copper amine oxidases (CAOs) catalyze the O(2)-dependent
16                                              Copper amine oxidases (CAOs) catalyze the two-electron o
17                                              Copper amine oxidases (CAOs) contain 2,4,5-trihydroxyphe
18                                    All known copper amine oxidases (CAOs) contain 2,4,5-trihydroxyphe
19 te specificity are investigated in a pair of copper amine oxidases (CAOs) from Hansenula polymorpha (
20                                          The copper amine oxidases (CAOs) have evolved to catalyze ox
21 ced cofactor to O2 in the catalytic cycle of copper amine oxidases (CAOs) remains controversial.
22 ridine (2HP) is an irreversible inhibitor of copper amine oxidases (CAOs).
23                                          The copper amine oxidases carry out two copper-dependent pro
24                                          The copper amine oxidases catalyze the O(2)-dependent, two-e
25                             Among these, the copper amine oxidases catalyze the oxidative deamination
26                                              Copper amine oxidases contain a buried protein-derived q
27                       At their active sites, copper amine oxidases contain both a mononuclear copper
28       Calculated O(2) free energy maps using copper amine oxidase crystal structures in the absence o
29                                              Copper amine oxidases (CuAOs) catalyze the oxidative dea
30  previously identified substrate analogue of copper amine oxidases (CuAOs) has been screened against
31 f the active site copper in Escherichia coli copper amine oxidase (ECAO), we initiated a metal-substi
32                                            A copper amine oxidase encoding gene, atao1, has been isol
33 gene At4g14940 (AtAO1) encodes an apoplastic copper amine oxidase expressed at the early stages of va
34 ivation is the subject of controversy in the copper amine oxidase family.
35 inker reversibly inhibit the activity of the copper amine oxidase from Arthrobacter globiformis (AGAO
36 rization of a cobalt-substituted form of the copper amine oxidase from Hansenula polymorpha (HPAO).
37 y conserved active site tyrosine Y305 in the copper amine oxidase from Hansenula polymorpha kinetical
38  wild-type and mutant forms of a recombinant copper amine oxidase from Hansenula polymorpha, expresse
39 ase in the aminotransferase mechanism of the copper amine oxidase from the yeast Hansenula polymorpha
40          The similar (18)O KIEs reported for copper amine oxidases from other sources raise the possi
41 cid polypeptide (ATAO1) with 48% identity to copper amine oxidases from pea and lentil.
42 e to variable experimental observations with copper amine oxidases from plant versus other eukaryotic
43                   In contrast to prokaryotic copper amine oxidases, however, it has not been possible
44  and steady state kinetic data of the second copper amine oxidase (HPAO-2) are presented for comparis
45 a-galactosidase and subsequently observed in copper amine oxidase, hyaluronate lyase, chondroitinase,
46             Lysyl oxidase differs from other copper amine oxidases in that its active quinone cofacto
47 droxyphenylalanine quinone (TPQ) cofactor in copper amine oxidases involves a key water addition to t
48                                              Copper amine oxidases oxidize the polyamine putrescine (
49 e general finding that the quinone-dependent copper amine oxidases specifically metabolize primary am
50 and tight binding fluorogenic substrate of a copper amine oxidase that is able to respond directly to
51 basis of the available crystal structures of copper amine oxidases, we propose that a histidine resid
52 e TPQ cofactor of wild-type Escherichia coli copper amine oxidase (WT-ECAO) is stable at neutral pH,

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