Abstract: The present invention relates to novel nuclear receptor ERR?3. Although ERR?3 itself lacks a DNA binding domain, it comprises the function of enhancing the transcriptional activation function of arbitrary nuclear receptors, such as ERR, ER, or TR. Moreover, the present inventors found that, like ERR?3, the known proteins ERR?1 and ERR?2 also comprise the function of enhancing the transcriptional activation function of other nuclear receptors. Thus, the present invention provides methods for evaluating the regulatory function of these ERR? subtypes in enhancing the transcriptional activation function of other nuclear receptors, and screening methods based on these evaluation methods.

Abstract: The present invention relates to the novel isoforms, RXR?2 and RXR?3, of nuclear receptor RXR?. Unlike known isoform RXR?1, the transcriptional activation functions of RXR?2 and RXR?3 are augmented by SRC-1. The present invention provides methods for evaluating the function of regulating augmentation by co-activators of these RXR? isoforms, and screening methods based on these evaluation methods. By controlling the interaction between isoforms and co-activators, transcription-controlling activity can be regulated in an isoform-specific manner.

Abstract: D-amino acid oxidase (DAO) originated from Fusarium solani M-0718, a DNA compound encoding the oxidase, expression vectors containing said DNA compound are provided. Esherichia coli transformants capable of producing recombinant DAO in high level are also provided.

Abstract: The present invention provides a process for producing 7-aminocephem compounds or salts thereof.

Abstract: D-amino acid oxidase (DAO) originated from Fusarium solani M-0718, a DNA compound encoding the oxidase, expression vectors containing said DNA compound are provided. Esherichia coli transformants capable of producing recombinant DAO in high level are also provided.

Abstract: A cephalosporin C acylase from Pseudomonas diminuta N-176 is characterized by its ability to catalyze the conversion of cephalosporin C, glutaryl 7-ACA, adipyl 7-ACA, succinyl 7-ACA, N-acetylcephalosporin, N-benzoylcephalosporin C and cephalothin into 7-aminocephalosporanic acid. The enzyme contains an .alpha.-subunit having a molecular weight of 26 kDA and a .beta.-subunit having a molecular weight of 58 kDa. A method for the recombinant production of the present cephalosporin C acylase in Escherichia coli is provided.

Abstract: A GL-7ACA acylase having the following characteristics:(a) has ability to catalyze the enzymatic conversion of glutaryl 7-ACA, adipyl 7-ACA, and succinyl 7-ACA, into 7-aminocephalosporanic acid,(b) has a molecular weight of 70,000 dalton (SDS-PAGE) and(c) has N-terminal amino acid sequence (sea in No: 1) thereof: Gln-Ser-Glu-Gln-Glu-Lys-Ala-Glu-Glu-.A process for producing GL-7ACA acylase is also provided.

Abstract: A GL-7ACA acylase having the following characteristics:(a) has ability to catalyze the enzymatic conversion of glutaryl 7-ACA, adipyl 7-ACA, and succinyl 7-ACA, into 7-aminocephalosporanic acid,(b) has a molecular weight of 70,000 dalton (SDS-PAGE) and(c) has N-terminal amino acid sequence (SEQ ID NO: 1) thereof: Gln-Ser-Glu-Gln-Glu-Lys-Ala-Glu-Glu-.A process for producing GL-7ACA acylase is also provided.

Abstract: A cephalosporin C acylase from Pseudomonas diminuta N-176 is disclosed as well as the recombinant production of this enzyme in E. coli. The enzyme is characterized by the ability to catalyze the conversion of cephalosporin C, gultaryl 7-ACA, apidyl 7-ACA, succinyl 7-ACA, N-acetylcephalosporin C, N-benzoylcephalosporin C, and cephalothin into 7-aminocephalosporanic acid and is composed of an .alpha.-subunit with a molecular weight of 26,000 daltons and a .beta.-subunit with a molecular weight of 58,000 daltons.