PMID- 16233841 OWN - NLM STAT- MEDLINE DCOM- 20051219 LR - 20061115 IS - 1389-1723 (Print) IS - 1347-4421 (Linking) VI - 99 IP - 6 DP - 2005 Jun TI - D-Amino acid dipeptide production utilizing D-alanine-D-alanine ligases with novel substrate specificity. PG - 623-8 AB - D-Alanine-D-alanine ligase (Ddl) is an important enzyme in the synthesis of bacterial peptidoglycan. The genes encoding Ddls from Escherichia coli K12 (EcDdlB), Oceanobacillus iheyensis JCM 11309 (OiDdl), Synechocystis sp. PCC 6803 (SsDdl) and Thermotoga maritima ATCC 43589 (TmDdl), the genomic DNA sequences of which have been determined, were cloned and the substrate specificities of these recombinant Ddls were investigated. Although OiDdl had a high substrate specificity for D-alanine; EcDdlB, SsDdl and TmDdl showed broad substrate specificities for D-serine, D-threonine, D-cysteine and glycine, in addition to D-alanine. Four D-amino acid dipeptides were produced using EcDdlB, and D-amino acid homo-dipeptides were successfully produced at high yields except for D-threonyl-D-threonine. FAU - Sato, Masaru AU - Sato M AD - Department of Applied Chemistry, School of Science and Engineering, Waseda University, 3-4-1 Ohkubo, Shinjuku-ku 169-8555, Tokyo, Japan. FAU - Kirimura, Kohtaro AU - Kirimura K FAU - Kino, Kuniki AU - Kino K LA - eng PT - Journal Article PT - Research Support, Non-U.S. Gov't PL - Japan TA - J Biosci Bioeng JT - Journal of bioscience and bioengineering JID - 100888800 RN - 0 (Dipeptides) RN - 0 (Recombinant Proteins) RN - EC 6.3.2.- (Peptide Synthases) RN - EC 6.3.2.4 (D-alanylalanine synthetase) SB - IM MH - Amino Acid Sequence MH - Cloning, Molecular MH - Dipeptides/*chemistry/*metabolism MH - Enzyme Activation MH - Escherichia coli/genetics/*metabolism MH - Molecular Sequence Data MH - Peptide Synthases/*chemistry/genetics/*metabolism MH - Protein Engineering/*methods MH - Recombinant Proteins/metabolism MH - Stereoisomerism MH - Substrate Specificity EDAT- 2005/10/20 09:00 MHDA- 2005/12/20 09:00 CRDT- 2005/10/20 09:00 PHST- 2005/01/24 00:00 [received] PHST- 2005/04/01 00:00 [accepted] PHST- 2005/10/20 09:00 [pubmed] PHST- 2005/12/20 09:00 [medline] PHST- 2005/10/20 09:00 [entrez] AID - S1389-1723(05)70418-7 [pii] AID - 10.1263/jbb.99.623 [doi] PST - ppublish SO - J Biosci Bioeng. 2005 Jun;99(6):623-8. doi: 10.1263/jbb.99.623.