PMID- 17090922
OWN - NLM
STAT- MEDLINE
DCOM- 20070130
LR  - 20061124
IS  - 0916-8451 (Print)
IS  - 0916-8451 (Linking)
VI  - 70
IP  - 11
DP  - 2006 Nov
TI  - Substrate specificity of thermostable D-alanine-D-alanine ligase from Thermotoga 
      maritima ATCC 43589.
PG  - 2790-2
AB  - D-Alanine-D-alanine ligase (Ddl) and its mutants maintain the biosynthesis of 
      peptidoglycan, and the substrate specificity of Ddls partially affects the 
      resistance mechanism of vancomycin-resistant enterococci. Through investigation 
      of Ddls, Ddl from Thermotoga maritima ATCC 43589 showed novel characteristics, 
      vis. thermostability up to 90 degrees C and broad substrate specificity toward 15 
      D-amino acids, particularly D-alanine, D-cysteine, and D-serine, in that order.
FAU - Sato, Masaru
AU  - Sato M
AD  - Department of Applied Chemistry, School of Science and Engineering, Waseda 
      University, Shinjuku-ku, 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
DEP - 20061107
PL  - England
TA  - Biosci Biotechnol Biochem
JT  - Bioscience, biotechnology, and biochemistry
JID - 9205717
RN  - EC 6.3.2.- (Peptide Synthases)
RN  - EC 6.3.2.4 (D-alanylalanine synthetase)
SB  - IM
MH  - Enzyme Stability
MH  - Peptide Synthases/genetics/*metabolism
MH  - Phylogeny
MH  - Substrate Specificity
MH  - Temperature
MH  - Thermotoga maritima/*enzymology/genetics
EDAT- 2006/11/09 09:00
MHDA- 2007/01/31 09:00
CRDT- 2006/11/09 09:00
PHST- 2006/11/09 09:00 [pubmed]
PHST- 2007/01/31 09:00 [medline]
PHST- 2006/11/09 09:00 [entrez]
AID - JST.JSTAGE/bbb/60307 [pii]
AID - 10.1271/bbb.60307 [doi]
PST - ppublish
SO  - Biosci Biotechnol Biochem. 2006 Nov;70(11):2790-2. doi: 10.1271/bbb.60307. Epub 
      2006 Nov 7.