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MetaCyc Enzyme: carboxynorspermidine dehydrogenase

Synonyms: CANSDH

Species: Vibrio alginolyticus NBRC 15630 = ATCC 17749

Subunit composition of carboxynorspermidine dehydrogenase = [carboxynorspermidine dehydrogenase subunit]2

Summary:
The native apparent molecular mass was determined by gel filtration chromatography [Nakao91].

This enzyme catalyzes the reductive condensation of L-aspartate-semialdehyde with propane-1,3-diamine or putrescine, which produces carboxynorspermidine, or carboxyspermidine, respectively. The latter compounds are intermediates in norspermidine or spermidine biosynthesis. The enzyme was was purified to homogeneity from extracts of Vibrio alginolyticus NBRC 15630 = ATCC 17749 and characterized. It was assigned the partial EC number 1.5.1.- [Nakao91].

Growth of Vibrio alginolyticus NBRC 15630 = ATCC 17749 in the presence of 5 mM norspermidine reduced the specific activity of this enzyme by approximately 70%, and also repressed two other enzymes in the biosynthetic pathway for norspermidine, L-2,4-diaminobutyrate decarboxylase and carboxynorspermidien decarboxylase [Nakao91]. See pathways norspermidine biosynthesis, spermidine biosynthesis II and superpathway of polyamine biosynthesis III.
The subunit apparent molecular mass was determined by SDS-PAGE [Nakao91].

Molecular Weight of Polypeptide: 45.1 kD (experimental) [Nakao91 ]

Molecular Weight of Multimer: 93.5 kD (experimental) [Nakao91]

Relationship Links: InterPro:IN-FAMILY:IPR005097 , InterPro:IN-FAMILY:IPR016040 , Pfam:IN-FAMILY:PF03435 , UniProt:Ortholog:Q1V6P7

Gene-Reaction Schematic: ?

Credits:
Created 09-Aug-2010 by Fulcher CA , SRI International


Enzymatic reaction of: carboxyspermidine dehydrogenase (carboxynorspermidine dehydrogenase)

EC Number: 1.5.1.43

L-aspartate-semialdehyde + putrescine + NADPH + H+ <=> carboxyspermidine + NADP+ + H2O

The reaction direction shown, that is, A + B ↔ C + D versus C + D ↔ A + B, is in accordance with the direction of enzyme catalysis.

The reaction is irreversible in the direction shown. [Nakao91]

Alternative Substrates for putrescine: propane-1,3-diamine [Nakao91 ]

In Pathways: superpathway of polyamine biosynthesis III , spermidine biosynthesis II

Summary:
In this reaction L-aspartate-semialdehyde serves as a carboxyaminopropyl group donor. The enzyme catalyzes the NADPH-linked reduction of the Schiff-base formed from L-aspartate-semialdehyde and putrescine, producing carboxyspermidine ([Nakao91] and in [Lee09d]).

putrescine was a much less efficient substrate than propane-1,3-diamine [Nakao91].


Enzymatic reaction of: carboxynorspermidine dehydrogenase

Synonyms: carboxynorspermidine synthase

EC Number: 1.5.1.43

L-aspartate-semialdehyde + propane-1,3-diamine + NADPH + H+ <=> carboxynorspermidine + NADP+ + H2O

The reaction direction shown, that is, A + B ↔ C + D versus C + D ↔ A + B, is in accordance with the direction of enzyme catalysis.

The reaction is irreversible in the direction shown. [Nakao91]

Alternative Substrates for NADPH: NADH [Nakao91 ]

Alternative Substrates for propane-1,3-diamine: putrescine [Nakao91 ]

In Pathways: superpathway of polyamine biosynthesis III , norspermidine biosynthesis

Summary:
In this reaction L-aspartate-semialdehyde serves as a carboxyaminopropyl group donor. The enzyme catalyzes the NADPH-linked reduction of the Schiff-base formed from L-aspartate-semialdehyde and propane-1,3-diamine, producing carboxynorspermidine ([Nakao91] and in [Lee09d]).

The enzyme was inhibited by sulfhydryl-reactive compounds [Nakao91].

putrescine was a much less efficient substrate than propane-1,3-diamine. Compounds that were not substrates included ethylenediamine, cadaverine, 1,2-diaminopropane and D-aspartate semialdehyde. NADH was a much less efficient cofactor than NADPH [Nakao91].

Activators (Unknown Mechanism): dithiothreitol [Nakao91]

Inhibitors (Unknown Mechanism): N-ethylmaleimide [Nakao91] , iodoacetamide [Nakao91]

Kinetic Parameters:

Substrate
Km (μM)
Citations
NADPH
1510.0
[Nakao91]

T(opt): 37 °C [Nakao91]

pH(opt): 7.25-7.5 [Nakao91]


References

Lee09d: Lee J, Sperandio V, Frantz DE, Longgood J, Camilli A, Phillips MA, Michael AJ (2009). "An alternative polyamine biosynthetic pathway is widespread in bacteria and essential for biofilm formation in Vibrio cholerae." J Biol Chem 284(15);9899-907. PMID: 19196710

Nakao91: Nakao H, Shinoda S, Yamamoto S (1991). "Purification and some properties of carboxynorspermidine synthase participating in a novel biosynthetic pathway for norspermidine in Vibrio alginolyticus." J Gen Microbiol 137(7);1737-42. PMID: 1955861


Report Errors or Provide Feedback
Please cite the following article in publications resulting from the use of MetaCyc: Caspi et al, Nucleic Acids Research 42:D459-D471 2014
Page generated by SRI International Pathway Tools version 18.5 on Thu Nov 27, 2014, BIOCYC14A.