Any feedback?
Information on EC 2.6.1.48 - 5-aminovalerate transaminase and Organism(s) Pseudomonas putida and UniProt Accession Q88RB9
for references in articles please use BRENDA:EC2.6.1.48Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
2.6.1.48 5-aminovalerate transaminaseIUBMB Comments
A pyridoxal-phosphate protein.
Specify your search results
Word Map
- 2.6.1.48
- semialdehyde
- l-lysine
- putida
- synthesis
- glutamicum
-
fed-batch
- aminotransferases
-
corynebacterium
The taxonomic range for the selected organisms is: Pseudomonas putida
The expected taxonomic range for this enzyme is: Bacteria, Archaea, Eukaryota
The expected taxonomic range for this enzyme is: Bacteria, Archaea, Eukaryota
Synonyms
pa0266, 5-aminovalerate transaminase, delta-aminovalerate aminotransferase, delta-aminovalerate transaminase, 5-aminovalerate aminotransferase, putative 5-aminovalerate aminotransferase, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
5-aminovalerate aminotransferase
-
-
-
-
delta-aminovalerate aminotransferase
-
-
-
-
delta-aminovalerate transaminase
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
amino group transfer
-
-
-
-
PATHWAY SOURCE
PATHWAYS
BRENDA
-
-, -, -, -
SYSTEMATIC NAME
IUBMB Comments
5-aminopentanoate:2-oxoglutarate aminotransferase
A pyridoxal-phosphate protein.
CAS REGISTRY NUMBER
COMMENTARY
37277-97-7
-
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
5-aminopentanoate + 2-oxoglutarate
5-oxopentanoate + L-glutamate
-
-
-
?
5-aminopentanoate + 2-oxoglutarate
5-oxovalerate + L-glutamate
-
-
r
5-aminopentanoate + 2-oxoglutarate
5-oxovalerate + L-glutamate
catabolism of lysine
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
5-aminopentanoate + 2-oxoglutarate
5-oxopentanoate + L-glutamate
-
-
-
?
5-aminopentanoate + 2-oxoglutarate
5-oxovalerate + L-glutamate
catabolism of lysine
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
metabolism
in the L-lysine catabolism pathway, 5-aminovaleric acid (5-AVA) is furter converted into glutarate semialdehyde by 5-aminovalerate transaminase encoded by davT
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
-
metabolic engineering of Corynebacterium glutamicum for the production of glutaric acid, a C5 dicarboxylic acid platform chemical, by co-expression of Pseudomonas putida davT, davB, and davD genes encoding lysine 2-monooxygenase, delta-aminovaleramidase, and glutarate semialdehyde dehydrogenase, respectively, in Corynebacterium glutamicum. Method optimization and evaluation. The glutaric acid biosynthesis pathway constructed in recombinant Corynebacterium glutamicum is engineered by examining strong synthetic promoters H30 and H36, Corynebacterium glutamicum codon-optimized davTDBA genes, and modification of davB gene with an N-terminal His6-tag to improve the production of glutaric acid. The use of N-terminal His6-tagged DavB is most suitable for the production of glutaric acid from glucose. Fed-batch fermentation on of the final engineered Corynebacterium glutamicum H30_GAHis strain, expressing davTDA genes along with davB fused with His6-tag at N-terminus can produce 24.5 g/l of glutaric acid with low accumulation of L-lysine (1.7 g/l), wherein 5-aminovaleric acid (5-AVA) ccumulation is not observed during fermentation. Metabolically engineered Corynebacterium glutamicum strain KCTC H30_GA-2 (engineered strain KCTC 1857) is able for catalysis of the biosynthesis of glutaric acid from glucose. Method optimization and evaluation, overview
additional information
metabolic engineering of Corynebacterium glutamicum for the production of glutaric acid, a C5 dicarboxylic acid platform chemical, by co-expression of Pseudomonas putida davT, davB, and davD genes encoding lysine 2-monooxygenase, delta-aminovaleramidase, and glutarate semialdehyde dehydrogenase, respectively, in Corynebacterium glutamicum. Method optimization and evaluation. The glutaric acid biosynthesis pathway constructed in recombinant Corynebacterium glutamicum is engineered by examining strong synthetic promoters H30 and H36, Corynebacterium glutamicum codon-optimized davTDBA genes, and modification of davB gene with an N-terminal His6-tag to improve the production of glutaric acid. The use of N-terminal His6-tagged DavB is most suitable for the production of glutaric acid from glucose. Fed-batch fermentation on of the final engineered Corynebacterium glutamicum H30_GAHis strain, expressing davTDA genes along with davB fused with His6-tag at N-terminus can produce 24.5 g/l of glutaric acid with low accumulation of L-lysine (1.7 g/l), wherein 5-aminovaleric acid (5-AVA) ccumulation is not observed during fermentation. Metabolically engineered Corynebacterium glutamicum strain KCTC H30_GA-2 (engineered strain KCTC 1857) is able for catalysis of the biosynthesis of glutaric acid from glucose. Method optimization and evaluation, overview
additional information
-
production of 5-aminovalerate and glutarate in Escherichia coli. Endogenous over-production of the precursor, lysine, is first achieved through metabolic deregulation of its biosynthesis pathway by introducing feedback resistant mutants of aspartate kinase III and dihydrodipicolinate synthase. Further disruption of native lysine decarboxylase activity limits cadaverine by-product formation. Co-expression of lysine monooxygenase and 5-aminovaleramide amidohydrolase then results in the production of 0.86 g/l 5-aminovalerate in 48 h. The additional co-expression of glutaric semialdehyde dehydrogenase and 5-aminovalerate aminotransferase leads to the production of 0.82 g/l glutarate under the same conditions. Yields on glucose are 71 and 68 mmol/mol for 5-aminovalerate and glutarate, respectively
additional information
-
metabolic engineering of Corynebacterium glutamicum for the production of glutaric acid, a C5 dicarboxylic acid platform chemical by co-expression with Pseudomonas putida dayA, dayB, and dayD genes encoding lysine 2-monooxygenase, delta-aminovaleramidase, and glutarate semialdehyde dehydrogenase, respectively, in Corynebacterium glutamicum. Method optimization and evaluation
additional information
metabolic engineering of Corynebacterium glutamicum for the production of glutaric acid, a C5 dicarboxylic acid platform chemical by co-expression with Pseudomonas putida dayA, dayB, and dayD genes encoding lysine 2-monooxygenase, delta-aminovaleramidase, and glutarate semialdehyde dehydrogenase, respectively, in Corynebacterium glutamicum. Method optimization and evaluation
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
gene davT identified using a transposon to generate transcriptional fusions by insertional mutagenesis
gene davT, recombinant expression of N-terminal His6-tagged enzyme in Corynebacterium glutamicum strain KCTC 1857, coexpression with glutarate semialdehyde dehydrogenase (davD, EC 1.2.1.20) from Pseudomonas putida, 4-aminobutyrate-2-oxoglutarate transaminase (gabT, EC 2.6.1.19) from Corynebacterium glutamicum, and NADP-dependent succinic semialdehyde dehydrogenase (gabD, EC 1.2.1.79) from Corynebacterium glutamicum, as well as N-terminal His6-tagged lysine 2-monooxygenase (davB, EC 1.13.12.2) from Pseudomonas putida
gene dayT, recombinant expression in Corynebacterium glutamicum, co-expression with Pseudomonas putida dayA, dayB, and dayD genes encoding lysine 2-monooxygenase, delta-aminovaleramidase, and glutarate semialdehyde dehydrogenase, respectively
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
synthesis
synthesis
-
production of 5-aminovalerate and glutarate in Escherichia coli. Endogenous over-production of the precursor, lysine, is first achieved through metabolic deregulation of its biosynthesis pathway by introducing feedback resistant mutants of aspartate kinase III and dihydrodipicolinate synthase. Further disruption of native lysine decarboxylase activity limits cadaverine by-product formation. Co-expression of lysine monooxygenase and 5-aminovaleramide amidohydrolase then results in the production of 0.86 g/l 5-aminovalerate in 48 h. The additional co-expression of glutaric semialdehyde dehydrogenase and 5-aminovalerate aminotransferase leads to the production of 0.82 g/l glutarate under the same conditions. Yields on glucose are 71 and 68 mmol/mol for 5-aminovalerate and glutarate, respectively
synthesis
-
production of 5-aminovalerate and glutarate in recombinant Escherichia coli. When the davAB genes encoding delta-aminovaleramidase and lysine 2-monooxygenase, respectively, are introduced into a recombinant Escherichia coli strain allowing enhanced L-lysine synthesis, 0.27 and 0.5 g/l of 5-aminovalerate are produced directly from glucose by batch and fed-batch cultures, respectively. Further conversion of 5-aminovalerate into glutarate can be demonstrated by expression of the Pseudomonas putida gabTD genes encoding 5-aminovalerate aminotransferase and glutarate semialdehyde dehydrogenase. A recombinant Eschrerichia coli strain expressing the davAB and gabTD genes cultured in a medium containing 20 g/l glucose,10 g/l L-lysine and 10 g/l alpha-ketoglutarate, produces 1.7 g/l of glutarate
synthesis
-
expression of the Pseudomonas putida davAB genes encoding delta-aminovaleramidase and lysine 2-monooxygenase, respectively, in Escherichia coli. When the davAB genes are introduced into recombinant E. coli strain XQ56 allowing enhanced L-lysine synthesis, 0.27 and 0.5g/l of 5-aminovalerate are produced directly from glucose by batch- and fed-batch cultures, respectively. Further conversion of 5-aminovalerate into glutarate can be achieved by expression of the Pseudomonas putida gabTD genes encoding 5-aminovalerate aminotransferase and glutarate semialdehyde dehydrogenase. In a medium containing 20g/l glucose, 10g/l L-lysine and 10g/l alpha-ketoglutarate, this strain produces 1.7g/l of glutarate
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Espinosa-Urgel, M.; Ramos, J.L.
Expression of a Pseudomonas putida aminotransferase involved in lysine catabolism is induced in the rhizosphere
Appl. Environ. Microbiol.
67
5219-5224
2001
Pseudomonas putida (Q88RB9), Pseudomonas putida
Adkins, J.; Jordan, J.; Nielsen, D.
Engineering Escherichia coli for renewable production of the 5-carbon polyamide building-blocks 5-aminovalerate and glutarate
Biotechnol. Bioeng.
110
1726-1734
2013
Pseudomonas putida, Pseudomonas putida KT 2240
Park, S.J.; Kim, E.Y.; Noh, W.; Park, H.M.; Oh, Y.H.; Lee, S.H.; Song, B.K.; Jegal, J.; Lee, S.Y.
Metabolic engineering of Escherichia coli for the production of 5-aminovalerate and glutarate as C5 platform chemicals
Metab. Eng.
16C
42-47
2012
Pseudomonas putida
Park, S.J.; Kim, E.Y.; Noh, W.; Park, H.M.; Oh, Y.H.; Lee, S.H.; Song, B.K.; Jegal, J.; Lee, S.Y.
Metabolic engineering of Escherichia coli for the production of 5-aminovalerate and glutarate as C5 platform chemicals
Metab. Eng.
16
42-47
2013
Pseudomonas putida, Pseudomonas putida ATCC 12633
Kim, H.T.; Khang, T.U.; Baritugo, K.A.; Hyun, S.M.; Kang, K.H.; Jung, S.H.; Song, B.K.; Park, K.; Oh, M.K.; Kim, G.B.; Kim, H.U.; Lee, S.Y.; Park, S.J.; Joo, J.C.
Metabolic engineering of Corynebacterium glutamicum for the production of glutaric acid, a C5 dicarboxylic acid platform chemical
Metab. Eng.
51
99-109
2019
Corynebacterium glutamicum (A0A0U4XQS6), Corynebacterium glutamicum, Pseudomonas putida, Pseudomonas putida (Q88RB9), Pseudomonas putida ATCC 47054 (Q88RB9), Pseudomonas putida DSM 6125 (Q88RB9), Pseudomonas putida NCIMB 11950 (Q88RB9)
EXTERNAL LINKS (specific for EC-Number 2.6.1.48)
Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.
Release 2023.1 (January 2023)
Legal
Curated at
Member of
