D
IPR001608

Alanine racemase, N-terminal

InterPro entry
Short nameAla_racemase_N
Overlapping
homologous
superfamilies
 
PLP-binding barrel (IPR029066)

Description

Alanine racemase plays a role in providing the D-alanine required for cell wall biosynthesis by isomerising L-alanine to D-alanine.

The molecular structure of alanine racemase from Bacillus stearothermophilus was determined by X-ray crystallography to a resolution of 1.9 A
[1]
. The alanine racemase monomer is composed of two domains, an eight-stranded α/β barrel at the N terminus, and a C-terminal domain essentially composed of β-strands. The pyridoxal 5'-phosphate (PLP) cofactor lies in and above the mouth of the α/β barrel and is covalently linked via an aldimine linkage to a lysine residue, which is at the C terminus of the first β-strand of the α/β barrel.

This N-terminal domain is also found in the PROSC (proline synthetase co-transcribed bacterial homologue) family of proteins, which are not known to have alanine racemase activity.

References

1.Determination of the structure of alanine racemase from Bacillus stearothermophilus at 1.9-A resolution. Shaw JP, Petsko GA, Ringe D. Biochemistry 36, 1329-42, (1997). View articlePMID: 9063881

Cross References

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