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Literature summary for 4.1.1.19 extracted from

  • Jantaro, S.; Kidron, H.; Chesnel, D.; Incharoensakdi, A.; Mulo, P.; Salminen, T.; Mäenpää, P.
    Structural modeling and environmental regulation of arginine decarboxylase in Synechocystis sp. PCC 6803 (2006), Arch. Microbiol., 184, 397-406 .
No PubMed abstract available
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Cloned(Commentary)

Cloned (Comment) Organism
gene ADC1, sequence comparisons Synechocystis sp. PCC 6803
gene ADC2, sequence comparisons Synechocystis sp. PCC 6803

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
L-arginine Synechocystis sp. PCC 6803
-
 agmatine + CO2
-
 ?

Organism

Organism UniProt Comment Textmining
Synechocystis sp. PCC 6803 P72587
-
-
Synechocystis sp. PCC 6803 P74576
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
L-arginine
-
 Synechocystis sp. PCC 6803 agmatine + CO2
-
 ?

Subunits

Subunits Comment Organism
dimer the enzyme dimer is stablized by the disulfide bridge involving Cys196 Synechocystis sp. PCC 6803

Synonyms

Synonyms Comment Organism
ADC
-
 Synechocystis sp. PCC 6803
ADC 1
-
 Synechocystis sp. PCC 6803
ADC 2
-
 Synechocystis sp. PCC 6803
biosynthetic arginine decarboxylase 1 UniProt Synechocystis sp. PCC 6803
biosynthetic arginine decarboxylase 2 UniProt Synechocystis sp. PCC 6803
slr0662
-
 Synechocystis sp. PCC 6803
slr1312
-
 Synechocystis sp. PCC 6803
SpeA
-
 Synechocystis sp. PCC 6803
speA1
-
 Synechocystis sp. PCC 6803
speA2
-
 Synechocystis sp. PCC 6803

Cofactor

Cofactor Comment Organism Structure
pyridoxal 5'-phosphate PLP, the PLP-binding domain is linked to the C-terminal domain by the N-terminus, structure modeling Synechocystis sp. PCC 6803

General Information

General Information Comment Organism
metabolism arginine decarboxylase (ADC) is the first enzyme in the alternative route to putrescine in the polyamine biosynthesis pathway, biosynthetic polyamine pathway, overview Synechocystis sp. PCC 6803
additional information residue Cys196 in ADC1 and ADC2 is highly conserved and involved in disulfide bonding. The putative disulfide bond in Synechocystis ADCs needs to be broken for catalytic activity. Synechocystis ADCs are posttranslationally regulated which might include the cleavage into two parts. In the model, the side chain of the arginine substrate can be bound by three aspartates, Asp521A, Asp548B, and Asp550B in ADC1 Synechocystis sp. PCC 6803
additional information residue Cys196 in ADC1 and ADC2 is highly conserved and involved in disulfide bonding. The putative disulfide bond in Synechocystis ADCs, formed by a highly conserved cysteine residue, needs to be broken for catalytic activity. Synechocystis ADCs are posttranslationally regulated which might include the cleavage into two parts. In the model, the side chain of the arginine substrate can be bound by three aspartates. Asp548B and Asp550B are probably important for substrate binding in ADCs Synechocystis sp. PCC 6803
physiological function the enzyme specific activity or the steady-state accumulation of ADC transcripts are markedly changed by photo-heterotrophic growth mode, salt stress under normal growth light or high-light intensity and stresses due to high temperature or iron deficiency. There is no general relationship between steady-state transcript accumulation and enzyme activity under the conditions studied, since both parameters are not regulated in a similar manner. The enzymatic activity of Synechocystis ADCs is posttranslationally regulated Synechocystis sp. PCC 6803