Date | Description | Acknowledgements |
---|---|---|
Jan 25, 2011 | New product name confidence: Class 2. New comment : Expressed as a hexa-histidine-tagged fusion in Escherichia coli BL21 Star (DE3). ALDHC in complex with NADPH bound in the cofactor binding pocket and an ordered fragment of a polyethylene glycol molecule bound in the substrate tunnel, to 1.6 A resolution. Belongs to space group P1. The ALDHC monomer comprises three distinct domains, an N-terminal cofactor (NAD/P+)-binding domain, a catalytic domain, and an oligomerization domain. New EC Number: 1.2.1.5. New GO Accession: GO:0004030(IDA). New PubMed reference: 18462753. | Literature review of BRENDA website by Geoffrey L. Winsor (Brinkman Lab). Simon Fraser University, Canada |
Jan 25, 2011 | New comment : ALDHC is preferentially active towards linear medium-chain to long-chain aldehydes as compared to branched-chain, short-chain or aromatic aldehydes. Reorientation of an extended loop (Asn478-Pro490) is responsible for the constricted structure of the substrate tunnel, with the side chain of Asn478 imposing steric restrictions on branched-chain and aromatic aldehydes. A key glycine (Gly104) positioned at the mouth of the tunnel allows for maximum tunnel depth required to bind the linear medium to long aliphatic chain of the native substrate. | Literature review of BRENDA website by Geoffrey L. Winsor (Brinkman Lab). Simon Fraser University, Canada |
Jan 25, 2011 | New product name confidence: Class 2. New EC Number: 1.2.1.5. New GO accession: GO:0004030 [IDA]. New evidence reference (PMID): 18462753. | Literature review of BRENDA website by Geoffrey L. Winsor (Brinkman Lab). Simon Fraser University, Canada |