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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.
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
9 e N assimilation pathway: the replacement of copper amine oxidase by a flavin-dependent backup enzyme
12 genesis of the topaquinone (TPQ) cofactor of copper amine oxidase (CAO) is self-catalyzed and require
19 te specificity are investigated in a pair of copper amine oxidases (CAOs) from Hansenula polymorpha (
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
33 gene At4g14940 (AtAO1) encodes an apoplastic copper amine oxidase expressed at the early stages of va
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
42 e to variable experimental observations with copper amine oxidases from plant versus other eukaryotic
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,
47 droxyphenylalanine quinone (TPQ) cofactor in copper amine oxidases involves a key water addition to t
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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