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Literature summary for 5.1.1.1 extracted from

  • Liu, S.; Wei, Y.; Zhou, X.; Zhang, K.; Peng, X.; Ren, B.; Chen, V.; Cheng, L.; Li, M.
    Function of alanine racemase in the physiological activity and cariogenicity of Streptococcus mutans (2018), Sci. Rep., 8, 5984 .
    View publication on PubMedView publication on EuropePMC
Search for more literature for 5.1.1.1

Application

Application Comment Organism
medicine Alr might be a potential target for the prevention and treatment of caries Streptococcus mutans serotype c

Cloned(Commentary)

Cloned (Comment) Organism
gene alr, quantitative RT-PCR expression analysis Streptococcus mutans serotype c

Protein Variants

Protein Variants Comment Organism
additional information upregulated expression of extracellular polysaccharide synthesis-associated genes in the alr-mutant group (genes gtfB, gtfC, and gtfD) according to quantitative RT-PCR expression analysis, and loosened biofilm with fewer cells but more extracellular matrix within the biofilms in the alr mutant. The mutant shows increased extracellular polysaccharide synthesis and decreased acid tolerance. Phenotype, overview. Decreased cariogenicity of alr-mutant strain in rats Streptococcus mutans serotype c

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
L-alanine Streptococcus mutans serotype c
-
 D-alanine
-
 r
L-alanine Streptococcus mutans serotype c ATCC 700610 / UA159
-
 D-alanine
-
 r

Organism

Organism UniProt Comment Textmining
Streptococcus mutans serotype c Q8DSF4
-
-
Streptococcus mutans serotype c ATCC 700610 / UA159 Q8DSF4
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
L-alanine
-
 Streptococcus mutans serotype c D-alanine
-
 r
L-alanine
-
 Streptococcus mutans serotype c ATCC 700610 / UA159 D-alanine
-
 r

Synonyms

Synonyms Comment Organism
ALR
-
 Streptococcus mutans serotype c

General Information

General Information Comment Organism
evolution two kinds of Alr have been identified in bacteria: the alr-encoded racemase, which is constitutive and used for D-Ala biosynthesis, and the dadX-encoded racemase, which is inducible and used for the catabolism of D-Ala Streptococcus mutans serotype c
malfunction lack of expression of the alr gene is lethal when there is no addition of exogenous D-Ala. Upregulated expression of extracellular polysaccharide synthesis-associated genes in the alr-mutant group (genes gtfB, gtfC, and gtfD) according to quantitative RT-PCR expression analysis, and loosened biofilm with fewer cells but more extracellular matrix within the biofilms in the alr mutant. The mutant shows increased extracellular polysaccharide synthesis and decreased acid tolerance. Decreased cariogenicity of alr-mutant strain in rats Streptococcus mutans serotype c
physiological function alanine racemase (Alr) is a bacterial enzyme that catalyses the conversion of L-Ala to D-Ala. This function is critical for the growth of bacteria due to their need for D-alanine, an essential component in the biosynthesis of cell wall peptidoglycan in both gram-positive and gram-negative bacteria2. Two kinds of Alr have been identified in bacteria: the alr-encoded racemase, which is constitutive and used for D-Ala biosynthesis, and the dadX-encoded racemase, which is inducible and used for the catabolism of D-Ala. Enzyme Alr is essential for the growth and interspecies competitiveness of Streptococcus mutans, the major causative organism of dental caries Streptococcus mutans serotype c