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Gene Review:

DNAH14 - dynein, axonemal, heavy chain 14

Homo sapiens

This record was replaced with 127602.

Yamazaki, H. et al., Yamazaki, H. et al., Little, J.M. et al.

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High impact information on DNAH14

Quinidine and anti-rat P450 2D1 antibody almost completely inhibited bufuralol 1'-hydroxylation in human sample HL-18 at a substrate concentration of 0.4 mM, whereas these effects were not so drastic when liver microsomes from human sample HL-67 were used [1].
Pentachlorophenol, an inhibitor of acetyltransferase activity, suppressed the activation of 6-aminochrysene in liver microsomes from phenobarbital-treated rats and from human samples HL-4, HL-13 and HL-18 but not HL-16 [2].
Detailed investigation of substrate specificity, using substrates representative of both the 1A (bilirubin, 4-nitrophenol) and 2B (androsterone, testosterone) families was carried out with HL32, HL38 (age and sex matched control) and HL18 (older control) [3].

Associations of DNAH14 with chemical compounds

In contrast, a very low concentration (< 10 microM) of alpha-naphthoflavone or anti-human P450 1A2 antibody significantly inhibited bufuralol 1'-hydroxylation catalyzed by human sample HL-67, but not HL-18, with 0.4 mM bufuralol [1].
In contrast, 1,1,1-trichloropropane-2,3-oxide, an inhibitor of epoxide hydrolase activity, enhanced the activation of 6-aminochrysene catalyzed by liver microsomes from beta-naphthoflavone-treated rats and from human samples HL-16 but not HL-4, HL-13 and HL-18 [2].

References

Bufuralol hydroxylation by cytochrome P450 2D6 and 1A2 enzymes in human liver microsomes. Yamazaki, H., Guo, Z., Persmark, M., Mimura, M., Inoue, K., Guengerich, F.P., Shimada, T. Mol. Pharmacol. (1994) [Pubmed]
Roles of different forms of cytochrome P450 in the activation of the promutagen 6-aminochrysene to genotoxic metabolites in human liver microsomes. Yamazaki, H., Mimura, M., Oda, Y., Inui, Y., Shiraga, T., Iwasaki, K., Guengerich, F.P., Shimada, T. Carcinogenesis (1993) [Pubmed]
Variability of human hepatic UDP-glucuronosyltransferase activity. Little, J.M., Lester, R., Kuipers, F., Vonk, R., Mackenzie, P.I., Drake, R.R., Frame, L., Radominska-Pandya, A. Acta Biochim. Pol. (1999) [Pubmed]

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