Molecular characterization of d-amino acid oxidase from common carp Cyprinus carpio and its induction with exogenous free d-alanine

Sarower, Mohammed Golam; Okada, Shigeru; Abe, Hiroki

doi:10.1016/j.abb.2003.09.035

Cited by 23 publications

(24 citation statements)

References 41 publications

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“…AY421707) was used as the starting materials for model building 14 . Comparative protein modelling requires at least one sequence of known experimental three-dimensional structure with a significant similarity to the target protein.…”

Section: Methodsmentioning

confidence: 99%

“…In view of the growing interest in the physiological functions of D-amino acids, DAO is also considered important in regulating the levels of Damino acids related to neural activity 15,16 . Several recent investigations revealed that DAO was respon- sible for metabolizing exogenous and endogenous free D-amino acids in animals 14,17 . DAO catalyses oxidative deamination of a variety of D-amino acids (Fig.…”

Section: Introductionmentioning

confidence: 99%

“…Since Krebs 11 discovered DAO in animal tissues, it has served as a subject for enzymological, biophysical, and medical investigations. The primary structure has been reported on the basis of the amino acid and nucleotide sequences of the cDNA [12][13][14] . In view of the growing interest in the physiological functions of D-amino acids, DAO is also considered important in regulating the levels of Damino acids related to neural activity 15,16 .…”

Section: Introductionmentioning

confidence: 99%

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Sarower¹,

Okada²,

Abe³

2009

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ABSTRACT:The three-dimensional structure of the flavoprotein D-amino acid oxidase (DAO, EC 1.4.3.3) from carp hepatopancreas (chDAO) and its active site cavity was modelled using ProModII. The structural features relevant for the overall conformation and for the catalytic activity are described. Secondary structure topology consists of 11 α-helices and 17 β-strands, which differs slightly from pig kidney, and Rhodotorula gracilis DAOs. chDAO showed a theoretical 'head-to-head' mode of dimerization. The presence of a short 'lid' in chDAO covering the active site, commonly found in mammalian DAO but absent in R. gracilis DAO, is interpreted as the origin of the differences in kinetic mechanism among these enzymes. This lid has been proposed to control the access of the substrate to the active site and to regulate dissociation of products. The conformational change in the large size active site loop determines the overall rate of turnover of DAOs. The shorter active site loop found in chDAO might be responsible for the higher turnover rate in chDAO compared to that of pkDAO.

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Section: Methodsmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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Sarower¹,

Okada²,

Abe³

2009

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“…No common trend of preference order of these enzymes toward D-amino acids has been found yet among mammals or microbes. Although primary structures of DAO or DDO from various sources are significantly different from each other, the catalytic residues in the active site are conserved [3][4][5][6][7][8][9][10][11] . The variation of DAO or DDO structures also provides different conformations of active site cavities 30 .…”

Section: Animal Animal Animal Animal Animalmentioning

confidence: 99%

“…On the basis of the common properties shared by these two enzymes and the homology of amino acid sequences, it has been suggested that they were derived from the divergent evolution of a single gene. The nucleotide sequences of DAO-encoding cDNAs have been determined in pig 3 , human 4 , mouse 5 , rabbit 6 , rat 7 , carp 8 and microbes 9 . On contrary DDO has been cloned only from beef kidney 10 and human brain 11 .…”

Section: Introductionmentioning

confidence: 99%

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Sarower¹,

Mizutani²,

Abe³

2004

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ABSTRACT:The distribution of D-amino acid oxidase (DAO, EC 1.4.3.3) and D-aspartate oxidase (DDO, EC 1.4.3.1) activities was examined on several tissues of various marine invertebrate species. Only DAO activity was detected in kidney and midgut gland from most of the mollusks with some exceptions. Hepatopancreas or liver from kuruma prawn, crayfish, squid, and octopus and antenal gland from crayfish showed significant amount of activity of both enzymes. Squid demonstrated a higher activity of DDO than that of DAO. DProline was the best substrate for DAO in common flying squid liver followed by D-alanine, D-histidine, Dtyrosine, and D-phenylalanine. On the contrary, meso-2,3-diaminosuccinate was the best substrate for DDO followed by N-acetyl-DL-aspartate, D-glutamate, D-amino adipate, and D-homocysteic acid. These enzymes, at least in kidney and midgut gland, are believed to metabolize exogenous and endogenous free D-alanine, that is abundant in aquatic invertebrates such as crustaceans and bivalve mollusks.

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