KEGG   ENZYME: 3.5.3.27
Entry
EC 3.5.3.27                 Enzyme                                 
Name
arginine dihydrolase;
argZ (gene name)
Class
Hydrolases;
Acting on carbon-nitrogen bonds, other than peptide bonds;
In linear amidines
Sysname
L-arginine aminodihydrolase (L-ornithine-forming)
Reaction(IUBMB)
L-arginine + 2 H2O = L-ornithine + CO2 + 2 ammonia [RN:R13308]
Reaction(KEGG)
R13308
Substrate
L-arginine [CPD:C00062];
H2O [CPD:C00001]
Product
L-ornithine [CPD:C00077];
CO2 [CPD:C00011];
ammonia [CPD:C00014]
Comment
The enzyme, characterized from different cyanobacterial species, is highly specific to arginine and does not require a metal cofactor. The enzyme from Nostoc is bifunctional, and also catalyses the activity of EC 4.3.1.12, ornithine cyclodeaminase.
History
EC 3.5.3.27 created 2024
Reference
1  [PMID:29632414]
  Authors
Zhang H, Liu Y, Nie X, Liu L, Hua Q, Zhao GP, Yang C.
  Title
The cyanobacterial ornithine-ammonia cycle involves an arginine dihydrolase.
  Journal
Nat Chem Biol 14:575-581 (2018)
DOI:10.1038/s41589-018-0038-z
  Sequence
[syn:sll1336]
Reference
2  [PMID:30636068]
  Authors
Burnat M, Picossi S, Valladares A, Herrero A, Flores E.
  Title
Catabolic pathway of arginine in Anabaena involves a novel bifunctional enzyme that produces proline from arginine.
  Journal
Mol Microbiol 111:883-897 (2019)
DOI:10.1111/mmi.14203
  Sequence
[ana:alr4995]
Reference
3  [PMID:31914412]
  Authors
Zhuang N, Zhang H, Li L, Wu X, Yang C, Zhang Y.
  Title
Crystal structures and biochemical analyses of the bacterial arginine dihydrolase ArgZ suggests a "bond rotation" catalytic mechanism.
  Journal
J Biol Chem 295:2113-2124 (2020)
DOI:10.1074/jbc.RA119.011752
  Sequence
[syn:sll1336]
Other DBs
ExplorEnz - The Enzyme Database: 3.5.3.27
IUBMB Enzyme Nomenclature: 3.5.3.27
ExPASy - ENZYME nomenclature database: 3.5.3.27
BRENDA, the Enzyme Database: 3.5.3.27

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