Group III pyridoxal-dependent decarboxylases

From Wikipedia, the free encyclopedia
Jump to: navigation, search
Orn/Lys/Arg decarboxylase, N-terminal domain
PDB 1ord EBI.jpg
crystallographic structure of a plp-dependent ornithine decarboxylase from lactobacillus 30a to 3.1 angstroms resolution
Identifiers
Symbol OKR_DC_1_N
Pfam PF03709
Pfam clan CL0304
InterPro IPR005308
PROSITE PDOC00585
SCOP 1ord
SUPERFAMILY 1ord
Orn/Lys/Arg decarboxylase, major domain
PDB 1ord EBI.jpg
crystallographic structure of a plp-dependent ornithine decarboxylase from lactobacillus 30a to 3.1 angstroms resolution
Identifiers
Symbol OKR_DC_1
Pfam PF01276
Pfam clan CL0061
InterPro IPR000310
PROSITE PDOC00585
SCOP 1ord
SUPERFAMILY 1ord
Orn/Lys/Arg decarboxylase, C-terminal domain
PDB 1ord EBI.jpg
crystallographic structure of a plp-dependent ornithine decarboxylase from lactobacillus 30a to 3.1 angstroms resolution
Identifiers
Symbol OKR_DC_1_C
Pfam PF03711
InterPro IPR008286
PROSITE PDOC00585
SCOP 1ord
SUPERFAMILY 1ord

In molecular biology, group III pyridoxal-dependent decarboxylases are a family of bacterial enzymes comprising ornithine decarboxylase EC 4.1.1.17, lysine decarboxylase EC 4.1.1.18 and arginine decarboxylase EC 4.1.1.19.[1]

Pyridoxal-5'-phosphate-dependent amino acid decarboxylases can be divided into four groups based on amino acid sequence. Group III comprises prokaryotic ornithine and lysine decarboxylase and the prokaryotic biodegradative type of arginine decarboxylase.[1]

Structure[edit]

These enzymes consist of several conserved domains. The N-terminal domain has a flavodoxin-like fold, and is termed the "wing" domain because of its position in the overall 3D structure. Ornithine decarboxylase from Lactobacillus 30a (L30a OrnDC) is representative of the large, pyridoxal-5'-phosphate-dependent decarboxylases that act on lysine, arginine or ornithine. The crystal structure of the L30a OrnDC has been solved to 3.0 A resolution. Six dimers related by C6 symmetry compose the enzymatically active dodecamer (approximately 106 Da). Each monomer of L30a OrnDC can be described in terms of five sequential folding domains. The amino-terminal domain, residues 1 to 107, consists of a five-stranded beta-sheet termed the "wing" domain. Two wing domains of each dimer project inward towards the centre of the dodecamer and contribute to dodecamer stabilisation.[2] The major domain contains a conserved lysine residue, which is the site of attachment of the pyridoxal-phosphate group.[2]

See also[edit]

References[edit]

  1. ^ a b Sandmeier E, Hale TI, Christen P (May 1994). "Multiple evolutionary origin of pyridoxal-5'-phosphate-dependent amino acid decarboxylases". Eur. J. Biochem. 221 (3): 997–1002. doi:10.1111/j.1432-1033.1994.tb18816.x. PMID 8181483. 
  2. ^ a b Momany C, Ernst S, Ghosh R, Chang NL, Hackert ML (October 1995). "Crystallographic structure of a PLP-dependent ornithine decarboxylase from Lactobacillus 30a to 3.0 A resolution". J. Mol. Biol. 252 (5): 643–55. doi:10.1006/jmbi.1995.0526. PMID 7563080. 

This article incorporates text from the public domain Pfam and InterPro IPR000310

This article incorporates text from the public domain Pfam and InterPro IPR005308

This article incorporates text from the public domain Pfam and InterPro IPR008286