The first identification and characterization of a histidine-specific amino acid racemase, histidine racemase from a lactic acid bacterium, Leuconostoc mesenteroides subsp. sake NBRC 102480

Amino Acids ◽  
2018 ◽  
Vol 51 (2) ◽  
pp. 331-343 ◽  
Author(s):  
Motoyasu Adachi ◽  
Rumi Shimizu ◽  
Shiro Kato ◽  
Tadao Oikawa
Author(s):  
Ryushi Kawakami ◽  
Chinatsu Kinoshita ◽  
Tomoki Kawase ◽  
Mikio Sato ◽  
Junji Hayashi ◽  
...  

Abstract The amino acid sequence of the OCC_10945 gene product from the hyperthermophilic archaeon Thermococcus litoralis DSM5473, originally annotated as γ-aminobutyrate aminotransferase, is highly similar to that of the uncharacterized pyridoxal 5ʹ-phosphate (PLP)-dependent amino acid racemase from Pyrococcus horikoshii. The OCC_10945 enzyme was successfully overexpressed in Escherichia coli by co-expression with a chaperone protein. The purified enzyme demonstrated PLP-dependent amino acid racemase activity primarily toward Met and Leu. Although PLP contributed to enzyme stability, it only loosely bound to this enzyme. Enzyme activity was strongly inhibited by several metal ions, including Co2+ and Zn2+, and non-substrate amino acids such as l-Arg and l-Lys. These results suggest that the underlying PLP-binding and substrate recognition mechanisms in this enzyme are significantly different from those of the other archaeal and bacterial amino acid racemases. This is the first description of a novel PLP-dependent amino acid racemase with moderate substrate specificity in hyperthermophilic archaea.


2012 ◽  
Vol 58 (3) ◽  
pp. 163-172 ◽  
Author(s):  
Jie Yu ◽  
Wa Gao ◽  
Manjun Qing ◽  
Zhihong Sun ◽  
Weihong Wang ◽  
...  

2013 ◽  
Vol 11 (4) ◽  
pp. 181-186 ◽  
Author(s):  
Yun-Seok Lee ◽  
Tae-Young Song ◽  
Won-Sik Kong ◽  
Min-Ho Yoon

2016 ◽  
Vol 54 ◽  
pp. 167-177 ◽  
Author(s):  
Fety Jaomanjaka ◽  
Olivier Claisse ◽  
Mélanie Blanche-Barbat ◽  
Melina Petrel ◽  
Patricia Ballestra ◽  
...  

2019 ◽  
Vol 64 (1) ◽  
pp. 71-78 ◽  
Author(s):  
Mohamed G. Shehata ◽  
Ahmed N. Badr ◽  
Sobhy A. El Sohaimy ◽  
Dalal Asker ◽  
Tarek S. Awad

2017 ◽  
Vol 26 (6) ◽  
pp. 1625-1632 ◽  
Author(s):  
Kamil Bostan ◽  
Ayla Unver Alcay ◽  
Semiha Yalçin ◽  
Ufuk Eren Vapur ◽  
Mustafa Nizamlioglu

2007 ◽  
Vol 51 (8) ◽  
pp. 2988-2990 ◽  
Author(s):  
Mariagrazia Perilli ◽  
Bibiana Caporale ◽  
Giuseppe Celenza ◽  
Cristina Pellegrini ◽  
Jean Denis Docquier ◽  
...  

ABSTRACT A new natural IND-type metallo-β-lactamase variant, IND-5, was identified in a clinical isolate of Chryseobacterium indologenes. IND-5 shared 92.8% and 92.4% amino acid homology with IND-1 and IND-3, respectively. Purified enzyme (pI = 8.8, M r = 25,000) was able to hydrolyze penicillins, some narrow- and expanded-spectrum cephalosporins, and carbapenems but not monobactams.


2016 ◽  
Vol 219 ◽  
pp. 3-4
Author(s):  
Gun-Seok Park ◽  
Sung-Jun Hong ◽  
Byung Kwon Jung ◽  
Changhee Lee ◽  
Choi Kyu Park ◽  
...  

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