KEGG   ENZYME: 2.5.1.161
Entry
EC 2.5.1.161                Enzyme                                 
Name
S-adenosyl-L-methionine:NAD+ aminocarboxypropyltransferase;
sbzP (gene name)
Class
Transferases;
Transferring alkyl or aryl groups, other than methyl groups;
Transferring alkyl or aryl groups, other than methyl groups (only sub-subclass identified to date)
Sysname
S-adenosyl-L-methionine:NAD+ aminocarboxypropyltransferase
Reaction(IUBMB)
S-adenosyl-L-methionine + NAD+ = S-methyl-5'-thioadenosine + (4aR,7S)-2-(adenosyl(5')diphospho(5)ribosyl)-7-amino-4-carbamoyl-4a,5,6,7-tetrahydro-2H-cyclopenta[c]pyridine-7-carboxylate [RN:R13435]
Reaction(KEGG)
R13435
Substrate
S-adenosyl-L-methionine [CPD:C00019];
NAD+ [CPD:C00003]
Product
S-methyl-5'-thioadenosine [CPD:C00170];
(4aR,7S)-2-(adenosyl(5')diphospho(5)ribosyl)-7-amino-4-carbamoyl-4a,5,6,7-tetrahydro-2H-cyclopenta[c]pyridine-7-carboxylate [CPD:C22998]
Comment
The enzyme, isolated from the bacterium Streptomyces sp. NCIMB40513, participates in the biosynthesis of the monoterpene alkaloids altemicidin, SB-203207 and SB-203208.The enzyme catalyses a pyridoxal phosphate-dependent [3+2]-annulation reaction between S-adenosyl-L-methionine (SAM) and NAD+. It transfers an aminocarboxypropyl group that combines with the pyridinium moiety of NAD+ to create a pentacyclic ring, forming a 6-azatetrahydroindane scaffold.
History
EC 2.5.1.161 created 2024
Orthology
K27980  S-adenosyl-L-methionine:NAD+ aminocarboxypropyltransferase
Reference
1  [PMID:34880494]
  Authors
Barra L, Awakawa T, Shirai K, Hu Z, Bashiri G, Abe I.
  Title
beta-NAD as a building block in natural product biosynthesis.
  Journal
Nature 600:754-758 (2021)
DOI:10.1038/s41586-021-04214-7
  Sequence
Other DBs
ExplorEnz - The Enzyme Database: 2.5.1.161
IUBMB Enzyme Nomenclature: 2.5.1.161
ExPASy - ENZYME nomenclature database: 2.5.1.161
BRENDA, the Enzyme Database: 2.5.1.161
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