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Information on EC 3.5.1.96 - succinylglutamate desuccinylase and Organism(s) Escherichia coli and UniProt Accession P76215

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IUBMB Comments
Requires Co2+ for maximal activity . N2-Acetylglutamate is not a substrate. This is the final enzyme in the arginine succinyltransferase (AST) pathway for the catabolism of arginine . This pathway converts the carbon skeleton of arginine into glutamate, with the concomitant production of ammonia and conversion of succinyl-CoA into succinate and CoA. The five enzymes involved in this pathway are EC 2.3.1.109 (arginine N-succinyltransferase), EC 3.5.3.23 (N-succinylarginine dihydrolase), EC 2.6.1.11 (acetylornithine transaminase), EC 1.2.1.71 (succinylglutamate-semialdehyde dehydrogenase) and EC 3.5.1.96 (succinylglutamate desuccinylase).
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Escherichia coli
UNIPROT: P76215
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The taxonomic range for the selected organisms is: Escherichia coli
The enzyme appears in selected viruses and cellular organisms
Synonyms
succinylglutamate desuccinylase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
PATHWAY SOURCE
PATHWAYS
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SYSTEMATIC NAME
IUBMB Comments
N-succinyl-L-glutamate amidohydrolase
Requires Co2+ for maximal activity [1]. N2-Acetylglutamate is not a substrate. This is the final enzyme in the arginine succinyltransferase (AST) pathway for the catabolism of arginine [1]. This pathway converts the carbon skeleton of arginine into glutamate, with the concomitant production of ammonia and conversion of succinyl-CoA into succinate and CoA. The five enzymes involved in this pathway are EC 2.3.1.109 (arginine N-succinyltransferase), EC 3.5.3.23 (N-succinylarginine dihydrolase), EC 2.6.1.11 (acetylornithine transaminase), EC 1.2.1.71 (succinylglutamate-semialdehyde dehydrogenase) and EC 3.5.1.96 (succinylglutamate desuccinylase).
CAS REGISTRY NUMBER
COMMENTARY hide
99676-40-1
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SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
N-succinyl-L-glutamate + H2O
succinate + L-glutamate
show the reaction diagram
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additional information
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only three enzymes of the ammonia-producing arginine succinyltransferase pathway can be measured in wild-type cells grown with ammonia as the sole nitrogen source: succinylarginine dihydrolase, succinylglutamate desuccinylase, and succinylornithine transaminase
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
mutant BW25113-DELTAastE mainly regulates intracellular pH-homeostasis to adapt to butanol stress, indicating the non-negligible impact of pH on microbial butanol tolerance, broadening our understanding of microbial butanol tolerance and providing a strategy for the rational engineering of a more robust butanol-producing host
metabolism
analysis of the mechanism of the enzyme's tolerance to butanol, metabolome and GC-MS-based transcriptomics analysis showing that acid-activated glutaminase ybaS and the amino acid antiporter gadC are significantly upregulated, but the levels of L-arginine and glutamate are not significantly increased and decreased, detailed overview
physiological function
final enzyme of the ammonia-producing arginine succinyltransferase pathway AST in Escherichia coli. Overproduction of AST enzymes results in faster growth with arginine and aspartate
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
construction of a butanol-tolerant Escherichia coli mutant strain BW25113-DELTAastE by disrupting gene astE (encoding succinylglutamate desuccinylase) to obtain higher butanol tolerance (increased by 34.6%). Analysis of the mechanism of increased tolerance to butanol in the mutant, overview. Mutant BW25113-DELTAastE mainly regulates intracellular pH-homeostasis to adapt to butanol stress, indicating the non-negligible impact of pH on microbial butanol tolerance, broadening our understanding of microbial butanol tolerance and providing a strategy for the rational engineering of a more robust butanol-producing host
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
gene astE, quantitative RT-PCR enzyme expression analysis
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
nitrogen limitation induces the enzymes of the ammonia-producing arginine succinyltransferase pathway AST. Maximal induction with arginine as the sole nitrogen source
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Schneider, B.L.; Kiupakis, A.K.; Reitzer, L.J.
Arginine catabolism and the arginine succinyltransferase pathway in Escherichia coli
J. Bacteriol.
180
4278-4286
1998
Escherichia coli (P76215)
Manually annotated by BRENDA team
Guo, Y.; Lu, B.; Tang, H.; Bi, D.; Zhang, Z.; Lin, L.; Pang, H.
Tolerance against butanol stress by disrupting succinylglutamate desuccinylase in Escherichia coli
RSC Adv.
9
11683-11695
2019
Escherichia coli (P76215), Escherichia coli BW25113 (P76215)
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Manually annotated by BRENDA team