Protein Family Models

This small three helical domain is found at the C-terminus of the arginine decarboxylase enzyme. [1]. 21139196. Structures of bacterial biosynthetic arginine decarboxylases. Forouhar F, Lew S, Seetharaman J, Xiao R, Acton TB, Montelione GT, Tong L;. Acta Crystallogr Sect F Struct Biol Cryst Commun. 2010;66:1562-1566. (from Pfam)

Date:

2024-10-16

This entry represents a helical bundle domain that is found between the two enzymatic domains of the arginine decarboxylases [1]. [1]. 20534592. Evolution of substrate specificity within a diverse family of beta/alpha-barrel-fold basic amino acid decarboxylases: X-ray structure determination of enzymes with specificity for L-arginine and carboxynorspermidine. Deng X, Lee J, Michael AJ, Tomchick DR, Goldsmith EJ, Phillips MA;. J Biol Chem. 2010;285:25708-25719. (from Pfam)

Date:

2024-10-16

These pyridoxal-dependent decarboxylases acting on ornithine, lysine, arginine and related substrates This domain has a TIM barrel fold. [1]. 10378276. Structure of mammalian ornithine decarboxylase at 1.6 A resolution: stereochemical implications of PLP-dependent amino acid decarboxylases. Kern AD, Oliveira MA, Coffino P, Hackert ML;. Structure Fold Des 1999;7:567-581. (from Pfam)

Date:

2024-10-16

arginine decarboxylase catalyzes the decarboxylation of L-arginine to agmatine in both PLP- and Mg2+-dependent manner

Date:

2017-02-03

Two alternative pathways can convert arginine to putrescine. One is decarboxylation by this enzyme followed by removal of the urea moeity by agmatinase. In the other, the ureohydrolase (arginase) acts first, followed by ornithine decarboxylase. This pathway leads to spermidine biosynthesis, hence the gene symbol speA. A distinct biodegradative form is also pyridoxal phosphate-dependent but is not similar in sequence.

Gene:

speA

Date:

2024-05-30

Catalyzes the formation of agmatine from arginine in putrescine and spermidine biosynthesis

Gene:

speA

Date:

2021-08-24