About: Group IV pyridoxal-dependent decarboxylases   Goto Sponge  NotDistinct  Permalink

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In molecular biology, group IV pyridoxal-dependent decarboxylases are a family of enzymes comprising ornithine decarboxylase EC 4.1.1.17, lysine decarboxylase EC 4.1.1.18, arginine decarboxylase EC 4.1.1.19 and diaminopimelate decarboxylaseEC 4.1.1.20. It is also known as the Orn/Lys/Arg decarboxylase class-II family.

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type
label
  • Group IV pyridoxal-dependent decarboxylases
comment
  • In molecular biology, group IV pyridoxal-dependent decarboxylases are a family of enzymes comprising ornithine decarboxylase EC 4.1.1.17, lysine decarboxylase EC 4.1.1.18, arginine decarboxylase EC 4.1.1.19 and diaminopimelate decarboxylaseEC 4.1.1.20. It is also known as the Orn/Lys/Arg decarboxylase class-II family.
sameAs
name
  • Pyridoxal-dependent decarboxylase, C-terminal sheet domain
  • Pyridoxal-dependent decarboxylase, pyridoxal binding domain
topic
depiction
  • External Image
  • External Image
described by
dbp:pfamClan
  • CL0036
subject
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is primary topic of
wasDerivedFrom
http://purl.org/li...ics/gold/hypernym
dbo:abstract
  • In molecular biology, group IV pyridoxal-dependent decarboxylases are a family of enzymes comprising ornithine decarboxylase EC 4.1.1.17, lysine decarboxylase EC 4.1.1.18, arginine decarboxylase EC 4.1.1.19 and diaminopimelate decarboxylaseEC 4.1.1.20. It is also known as the Orn/Lys/Arg decarboxylase class-II family. Pyridoxal-5'-phosphate-dependent amino acid decarboxylases can be divided into four groups based on amino acid sequence. Group IV comprises eukaryotic ornithine and lysine decarboxylase and the prokaryotic biosynthetic type of arginine decarboxylase and diaminopimelate decarboxylase. Members of this family while most probably evolutionary related, do not share extensive regions of sequence similarities. The proteins contain a conserved lysine residue which is known, in mouse ODC to be the site of attachment of the pyridoxal-phosphate group. The proteins also contain a stretch of three consecutive glycine residues and has been proposed to be part of a substrate-binding region.
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  • a dimer interface mutant of ornithine decarboxylase reveals structure of gem diamine intermediate
  • crystal structure of a d,l-lysine complex of diaminopimelate decarboxylase
dbp:symbol
  • Orn_Arg_deC_N
  • Orn_DAP_Arg_deC
dbp:interpro
  • IPR022643
  • IPR022644
dbp:pfam
  • PF00278
  • PF02784
dbp:prosite
  • PDOC00685
dbp:scop
dbo:symbol
  • Orn_Arg_deC_N
  • Orn_DAP_Arg_deC
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