Member database | PROSITE patterns |
PROSITE patterns type | conserved site |
Short name | DALA_DALA_LIGASE_1 |
Description
D-alanine--D-alanine ligase (EC 6.3.2.4) is a bacterial enzyme involved in
cell-wall biosynthesis. It participates in forming UDP-N-acetylmuramyl
pentapeptide, the peptidoglycan precursor.
In Escherichia coli and related bacteria, there are two different D-ala--D-ala
ligase isozymes (genes ddlA and ddlB)
[1]. In Enterobacterium faecium and
gallinarum, genes vanA and vanC encode D-ala--D-ala ligases of altered
specificity, which catalyze ester bond formations between D-ala and various
D-hydroxy acids [2]. They are required for resistance to glycopeptide
antibiotics, such as vancomycin which inhibits late stages in cell-wall
synthesis.
These enzymes are proteins of 300 to 360 amino acids. There are many
conserved regions, of which we selected two as signature patterns. The first
pattern, which is Gly-rich and could be involved in ATP-binding, is located
near the N-terminal extremity, the second is in the C-terminal section.
References
1.Existence of two D-alanine:D-alanine ligases in Escherichia coli: cloning and sequencing of the ddlA gene and purification and characterization of the DdlA and DdlB enzymes. Zawadzke LE, Bugg TD, Walsh CT. Biochemistry 30, 1673-82, (1991). View articlePMID: 1993184