Sequence and characteristics of the Bifidobacterium longum gene encoding l-lactate dehydrogenase and the primary structure of the enzyme: a new feature of the allosteric site-Reference-Cited by-同舟云学术

Sequence and characteristics of the Bifidobacterium longum gene encoding l-lactate dehydrogenase and the primary structure of the enzyme: a new feature of the allosteric site

Published:1989-12 Issue:1 Volume:85 Page:161-168
ISSN:0378-1119
Container-title:Gene
language:en
Short-container-title:Gene

Author:

Takashi Minowa,So Iwata,Hiroshi Sakai,Haruhiko Masaki,Takahisa Ohta

Publisher

Elsevier BV

Subject

Genetics,General Medicine

Reference21 articles.

1. Evidence for two functional gal promoters in intact Escherichia coli cells;Aiba;J. Biol. Chem.,1981

2. Cloning, expression and complete nucleotide sequence of the Bacillus stearothermophilusl-lactate dehydrogenase gene;Barstow;Gene,1986

3. Crystallization and preliminary crystallographic analysis at low resolution of the allosteric l-lactate dehydrogenase from Lactobacillus casei;Buehner;J. Mol. Biol.,1982

4. A single amino acid substitution deregulates a bacterial lactate dehydrogenase and stabilizes its tetrameric structure;Clarke;Biochem. Biophys. Acta,1987

5. Structural adaptations of lactate dehydrogenase isozymes;Eventoff,1977

Cited by 46 articles. 订阅此论文施引文献订阅此论文施引文献，注册后可以免费订阅5篇论文的施引文献，订阅后可以查看论文全部施引文献

1. Bifidobacterium species associated with breastfeeding produce aromatic lactic acids in the infant gut;Nature Microbiology;2021-10-21

2. Breastmilk-promoted bifidobacteria produce aromatic amino acids in the infant gut;2020-01-23

3. Comparative Genomics Reveals the Regulatory Complexity of Bifidobacterial Arabinose and Arabino-Oligosaccharide Utilization;Frontiers in Microbiology;2018-04-24

4. A molecular design that stabilizes active state in bacterial allosteric L-lactate dehydrogenases;Journal of Biochemistry;2011-08-09

5. Molecular genetic characterization of the thermostable L-lactate dehydrogenase gene (ldhL) of Thermoanaerobacter ethanolicus JW200 and biochemical characterization of the enzyme;Biochemistry (Moscow);2010-04