Amino acid sequence alignment oxidases

Knowledge of the three-dimensional structure of ascorbate oxidase and of amino-acid sequences of all members of the blue oxidases made it possible to carry out a structurally based amino-acid sequence alignment 101) involving N. crassa laccase, cucumber ascorbate oxidase, and human ceruloplasmin. The structural basis of this alignment was... 

In the trimer of nitrite reductase a six-domain structure is realized, which is reminiscent of the six-domain structure of ceruloplasmin (112), which was deduced from the amino-acid sequence alignment with the other blue oxidases (101). However, the arrangement of the six gene segments in ceruloplasmin is not simply a triplication of an ancestral... 

Structurally Based Amino-Acid Sequence Alignment of Fungal Laccases, Ascorbate Oxidases, and Related Proteins "... 

A structurally based amino-acid sequence alignment strongly suggests a three-domain structure for laccase, closely related to ascorbate oxidase, and a six-domain structure for ceruloplasmin. These domains demonstrate homology with the small blue copper proteins. The relationship suggests that laccase, like ascorbate oxidase, has a mononuclear blue copper in domain 3 and a trinuclear copper between domain 1 and domain 3, and ceruloplasmin has mononuclear copper ions in domains 2, 4, and 6 and a trinuclear copper between domain 1 and domain 6. 

Fig. 4. Sequence alignment of flavocytochromes 62 and glycollate oxidase. The amino acid sequences of the mature forms of flavocytochromes 62 from Saccharomyces cerevisiae (Scb2) and Hansenula anomala (Hab2) and of glycollate oxidase from spinach (SpGO) are shown along with a consensus (Con) wherein all three sequences are identical. The interdomain hinge region and the proteinase-sensitive loop of flavocytochromes are boxed.

Table 1. Alignment of amino acid sequences of several copper amine oxidase around the position of topa quinone. The sequences were obtained by translation the corresponding cDNAs except for the enzymes from porcine kidney and porcine serum and the benzylamine oxidase from Hansenula polymorpha where they were determined by automated Edman degradation of peptides. Homologous consensus sequence around the cofactor is underlined, the tyrosyl precursor of topa quinone is shown as y.

FIGURE 2. Alignment of the deduced amino acid sequences of GLO, 6-hydroxy-D-nicotine oxidase (6-HDNO), mcrA protein (MCRA), and berberine bridge enzyme (reticuline oxidase) (BBE). Identical residues are boxed. Arrowhead indicates the position of the histidyl residue to which FAD is covalently bound in 6-hydroxy-D-nicotine oxidase. Adapted from Brandsch (1994) and August et al. (1994). 

Figure 4 Sequence alignment of the N-termini of AroA and molybdenum-containing proteins. The sequences belong to the arsenite oxidase of NT-26 (NT-26 AroA), the formate dehydrogenase of Wolinella succinogenes (W.s. FdhA), and the nitrate-inducible formate dehydrogenase of Escherichia coli (E.c. FdnG). Boxed amino acids show identity to NT-26 AroA.

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