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KMID : 0043319970200060590
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Archives of Pharmacal Research
1997 Volume.20 No. 6 p.590 ~ p.596
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Purification of the NADH Reductase Component of the Steroid -hydroxylase from Mycobacterium fortuitum
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Kang Hee-Kyoung
Lee Sang-Sup
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Abstract
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The NADH reductase component of the steroid 9.alpha.-hydroxylase from Mycobacterium fortuitum was purified to homogeneity. Recovery of the enzyme from the 50-60% ammonium sulfate saturated fraction was 49%, with a purification factor of 100-fold. The NADH reductase has a relative molecular of 60 KDa as determined by SDS-PAGE. The absorption maxima at 410 and 450 nm indicate the presence of iron-sulfur group and flavin. These prosthetic groups seemed to function as redox groups that transfer electrons from NADH to the following protein. The value for NADH as substrate was . The -terminal amino acid sequence of the reductase was determined as Met-Asp-Ala-Ile-Thr-Asn-Val-Pro-Leu-Pro-Ala-Asn-Glu-Pro-Val-His-Asp-Tyr-Ala-Thr. This sequence does not show a homology with the -terminal sequences reported for the reductase component of other monooxygenases, suggesting that the NADH reductase component of the steroid 9.alpha.-hydroxylase system is novel.
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KEYWORD
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Steroid 9a-hydroxylase, NADH reductase component, Iron-sulfur group and flavin
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