B6db families : 5_1_1

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5.1.1.18

Activity

5.1.1.18

Description

Serine racemase

Notes

Validated eukaryotic enzymes (from metazoa and plants) are similar in sequence to serine ammonia-lyases (4.3.1.17), and in fact they often catalyze dehydration of serine to pyruvate in addition to serine racemization.

In bacteria amino acid racemization is usually carried out by fold-type III enzymes (that we have grouped in the 5.1.1.1 family).
One bacterial enzyme with a sequence similar to those herein and showing some serine racemase activity (WP_013961474 from Roseobacter litoralis; see Kubota et al. 2016, Microbiology 162 53-61) is probably acting physiologically as an erythro-3-hydroxy-D-aspartate ammonia-lyase (family bhcb), as suggested by the genomic context.

PLP Fold Type

PLP-dependent Domain

Domain alignment
Domain hmm

Fold type II

Reference sequence

SRR_HUMAN

Domain interval

19-314

Catalytic site

56 K

References

Katane M, Saitoh Y, Uchiyama K, Nakayama K, Saitoh Y, Miyamoto T, Sekine M, Uda K, Homma H (2016) Characterization of a homologue of mammalian serine racemase from Caenorhabditis elegans: the enzyme is not critical for the metabolism of serine in vivo Genes Cells 21 966-77.

Kubota T, Shimamura S, Kobayashi T, Nunoura T, Deguchi S (2016) Distribution of eukaryotic serine racemases in the bacterial domain and characterization of a representative protein in Roseobacter litoralis Och 149 Microbiology 162 53-61.

Uda K, Abe K, Dehara Y, Mizobata K, Sogawa N, Akagi Y, Saigan M, Radkov AD, Moe LA. (2016) Distribution and evolution of the serine/aspartate racemase family in invertebrates Amino Acids 48 387-402.

Ito T, Murase H, Maekawa M, Goto M, Hayashi S, Saito H, Maki M, Hemmi H, Yoshimura T. (2012) Metal ion dependency of serine racemase from Dictyostelium discoideum. Amino Acids. 43 1567-76.

Fujitani Y; Horiuchi T; Ito K.; Sugimoto M. (2007) Serine racemases from barley, Hordeum vulgare L., and other plant species represent a distinct eukaryotic group: gene cloning and recombinant protein characterization Phytochemistry 68 1530-6.

Fujitani, Y.; Nakajima, N.; Ishihara, K.; Oikawa, T.; Ito, K.; Sugimoto, M. (2006) Molecular and biochemical characterization of a serine racemase from Arabidopsis thaliana Phytochemistry 67 668-674.

De Miranda, J.; Santoro, A.; Engelender, S.; Wolosker, H. (2000) Human serine racemase: moleular cloning, genomic organization and functional analysis Gene 256 183-8.

Articles on 5.1.1.18

last changed

2019/11/20 17:14