Elsevier

Genomics

Volume 52, Issue 1, 15 August 1998, Pages 95-100
Genomics

Short Communication
Mapping of a Novel Human Carbonyl Reductase, CBR3, and Ribosomal Pseudogenes to Human Chromosome 21q22.2

https://doi.org/10.1006/geno.1998.5380Get rights and content

Abstract

To find the genes contributing to Down syndrome, we constructed a 4-Mb sequence-ready map spanning chromosome 21q22.2 with megabase-sized cosmid/P1-derived artificial chromosome (PAC) contigs. The restriction map with rare cutting enzymes, followed by sequencing from the clustering sites, has defined CpG islands and revealed the genes associated with CpG islands (Accession No. D85771). Of these, two human carbonyl reductases (CBR; EC1.1.1.184) were found in a PAC 25P16 clone. CBR catalyzes the reduction of a large number of biologically and pharmacologically active carbonyl compounds to their corresponding alcohols and has been mapped in 21q22.1. To confirm these results, we sequenced the PAC clone in shotgun strategies and identified a novel carbonyl reductase, designated CBR3, 62 kb downstream from the original CBR. In addition, three ribosomal pseudogenes, L23a, S9, and L3, and some cDNAs with ESTs were mapped in the sequence. In conclusion, the sequence analysis for CpG islands predicted from the megabase-sized contigs will reveal and identify the genes involved in Down syndrome.

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    2012, Biochemical and Biophysical Research Communications
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    So far, three carbonyl reductases (CBRs) have been identified in humans (CBR1 [SDR21C1], CBR3 [SDR21C2] and CBR4 [SDR45C1]) all of which belong to the short-chain dehydrogenase/reductase (SDR) superfamily [2]. Since the identification of CBR3 in 1998 [3] some progress has been made with regard to its tissue-specific distribution, but still the understanding of its molecular function is incomplete [4]. Although being considered an enzyme in the reductive metabolism of anthracyclines such as doxorubicin and daunorubicin [5,6], the poor catalytic efficiencies for other tested carbonyl compounds imply that the expected function of CBR3 in xenobiotic carbonyl metabolism is very unlikely [7,8].

  • Analysis of the substrate-binding site of human carbonyl reductases CBR1 and CBR3 by site-directed mutagenesis

    2009, Chemico-Biological Interactions
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    The regulation of CBR1 is described in Ref. [18]. In contrast, CBR3 was discovered only recently, its gene has been identified in 1998 [19] and its physiological role is still unknown. Thanks to the availability of experimentally determined structures of the enzymes, the comparison of the catalytic clefts could shed light on the different substrate specificity.

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Sequence data from this article have been deposited with the DDBJ, EMBL, and GenBank Data Libraries under Accession Nos. AB003151 and AB004848–AB004854.

1

To whom correspondence and reprint requests should be addressed. Telephone: 81-298-36-9122. Fax: 81-298-36-9140. E-mail:[email protected].

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