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Information on EC 3.5.1.30 - 5-aminopentanamidase
for references in articles please use BRENDA:EC3.5.1.30
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EC Tree 3 Hydrolases
3.5 Acting on carbon-nitrogen bonds, other than peptide bonds
3.5.1 In linear amides
3.5.1.30 5-aminopentanamidase
IUBMB Comments
The enzyme from Pseudomonas putida also acts on 4-aminobutanamide and, more slowly, on 6-aminohexanamide.
The expected taxonomic range for this enzyme is: Bacteria, Archaea
- 3.5.1.30
- putida
- 5-aminovalerate
- l-lysine
-
fed-batch
- glutarate
-
2-monooxygenase
- glutamicum
- transaminase
-
corynebacterium
- semialdehyde
-
nylon
-
bio-based
-
codon-optimized
- 1,5-pentanediol
-
proof-of-concept
- aminotransferase
- biomass
-
his6-tagged
- synthesis
showSynonyms
delta-aminovaleramidase, 5-aminovaleramidase, more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
5-aminonorvaleramidase
-
-
-
-
5-aminovaleramidase
5-aminovaleramide amidase
DavA
delta-aminovaleramidase
5-aminovaleramidase
-
-
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
5-aminopentanamide + H2O = 5-aminopentanoate + NH3
-
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of amide bond
-
-
-
-
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PATHWAY SOURCE
PATHWAYS
BRENDA
MetaCyc
L-lysine degradation IV
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SYSTEMATIC NAME
IUBMB Comments
5-aminopentanamide amidohydrolase
The enzyme from Pseudomonas putida also acts on 4-aminobutanamide and, more slowly, on 6-aminohexanamide.
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CAS REGISTRY NUMBER
COMMENTARY
9054-60-8
-
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
4-aminobutyramide + H2O
4-aminobutanoate + NH3
-
Substrates: -
Products: -
Products: -
?
4-aminobutyramide + H2O
4-aminobutanoate + NH3
-
Substrates: -
Products: -
Products: -
?
5-aminopentanamide + H2O
5-aminopentanoate + NH3
-
Substrates: -
Products: -
Products: -
?
5-aminopentanamide + H2O
5-aminopentanoate + NH3
Substrates: -
Products: -
Products: -
?
5-aminopentanamide + H2O
5-aminopentanoate + NH3
-
Substrates: -
Products: -
Products: -
?
5-aminopentanamide + H2O
5-aminopentanoate + NH3
Substrates: -
Products: -
Products: -
?
5-aminopentanamide + H2O
5-aminopentanoate + NH3
Substrates: -
Products: -
Products: -
r
5-aminopentanamide + H2O
5-aminopentanoate + NH3
Substrates: -
Products: -
Products: -
?
5-aminopentanamide + H2O
5-aminopentanoate + NH3
Substrates: -
Products: -
Products: -
r
5-aminopentanamide + H2O
5-aminopentanoate + NH3
Substrates: -
Products: -
Products: -
?
5-aminopentanamide + H2O
5-aminopentanoate + NH3
-
Substrates: -
Products: -
Products: -
?
5-aminopentanamide + H2O
?
-
Substrates: known intermediate in lysine catabolism
Products: -
Products: -
?
6-aminohexanamide + H2O
6-aminohexanoate + NH3
-
Substrates: -
Products: -
Products: -
?
6-aminohexanamide + H2O
6-aminohexanoate + NH3
-
Substrates: -
Products: -
Products: -
?
methyl-delta-aminovalerate + H2O
5-aminopentanoate + methanol
-
Substrates: -
Products: -
Products: -
?
methyl-delta-aminovalerate + H2O
5-aminopentanoate + methanol
-
Substrates: -
Products: -
Products: -
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
5-aminopentanamide + H2O
5-aminopentanoate + NH3
Substrates: -
Products: -
Products: -
?
5-aminopentanamide + H2O
5-aminopentanoate + NH3
-
Substrates: -
Products: -
Products: -
?
5-aminopentanamide + H2O
5-aminopentanoate + NH3
Substrates: -
Products: -
Products: -
?
5-aminopentanamide + H2O
5-aminopentanoate + NH3
Substrates: -
Products: -
Products: -
r
5-aminopentanamide + H2O
5-aminopentanoate + NH3
Substrates: -
Products: -
Products: -
?
5-aminopentanamide + H2O
5-aminopentanoate + NH3
Substrates: -
Products: -
Products: -
r
5-aminopentanamide + H2O
5-aminopentanoate + NH3
Substrates: -
Products: -
Products: -
?
5-aminopentanamide + H2O
?
-
Substrates: known intermediate in lysine catabolism
Products: -
Products: -
?
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Cd2+
-
0.5 mM, complete inhibition , characteristic of enzymes with essential vicinal sulfhydryl groups
arsenite
-
characteristic of enzymes with essential vicinal sulfhydryl groups
p-hydroxymercuribenzoate
-
0.00025 mM, 44% inhibition, inhibition partially reversed by dithioerythritol
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
30
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
Highest Expressing Human Cell Lines
Cell Line LinksPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
metabolism
metabolism
5-aminovalerate, produced by the enzyme DavA, is an intermediate of L-lysine catabolism that is called aminovalerate pathway in Pseudomonas putida
metabolism
metabolic pathway design for the recombinant production of 5-aminovalerate and glutarate in Corynebacterium glutamicum starting from the pathway precursor L-lysine and involving 5-aminovaleramide amidase, overview
metabolism
-
metabolic pathway design for the recombinant production of 5-aminovalerate and glutarate in Corynebacterium glutamicum starting from the pathway precursor L-lysine and involving 5-aminovaleramide amidase, overview
-
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UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). A0A3G7BSM8_9PSED
264
0
29217
TrEMBL
-
A0A6J4SKU9_9ACTN
259
0
27068
TrEMBL
-
A0A1L3L5U4_9HYPH
259
0
27413
TrEMBL
-
Q88QV2_PSEPK
Pseudomonas putida (strain ATCC 47054 / DSM 6125 / CFBP 8728 / NCIMB 11950 / KT2440)
264
0
29311
TrEMBL
-
A0A6J4TLJ6_9ACTN
273
0
27867
TrEMBL
-
A0A068MZA9_SYNY4
321
0
35443
TrEMBL
-
F2RCI1_STRVP
Streptomyces venezuelae (strain ATCC 10712 / CBS 650.69 / DSM 40230 / JCM 4526 / NBRC 13096 / PD 04745)
268
0
28200
TrEMBL
-
A0A0S2W0Y2_9FIRM
304
0
34028
TrEMBL
-
A0A150LLA9_9BACI
266
0
30234
TrEMBL
-
A0A6J4TCD8_9ACTN
263
0
27495
TrEMBL
-
A0A0J9E4W2_9RHOB
260
0
27844
TrEMBL
-
A0A6J4XYZ3_9DELT
264
0
29058
TrEMBL
-
A0A3G7LR65_9PSED
264
0
29235
TrEMBL
-
A0A7I8MXF8_9DELT
269
0
29862
TrEMBL
-
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
combined expression of Pseudomonas putida davB and davA genes encoding lysine 2-monooxygenase and delta-aminovaleramidase, respectively, in engineered Corynebacterium glutamicum strain BE (KCTC 12390BP) for large scale production of 5-aminovalerate (5AVA) under the control of constitutive promoters. Expression of codon-optimized N-terminally His6-tagged davA gene fused the davB gene as an operon under a strong synthetic H36 promoter from plasmid p36davAB3 in Corynebacterium glutamicum in fed-batch culture enables the most efficient production of 5AVA. In addition, production of glutaric acid, a major byproduct, is significantly reduced by employing Corynebacterium glutamicum gabT mutant as a host. Method development and optimization, overview
additional information
-
combined expression of Pseudomonas putida davB and davA genes encoding lysine 2-monooxygenase and delta-aminovaleramidase, respectively, in engineered Corynebacterium glutamicum strain BE (KCTC 12390BP) for large scale production of 5-aminovalerate (5AVA) under the control of constitutive promoters. Expression of codon-optimized N-terminally His6-tagged davA gene fused the davB gene as an operon under a strong synthetic H36 promoter from plasmid p36davAB3 in Corynebacterium glutamicum in fed-batch culture enables the most efficient production of 5AVA. In addition, production of glutaric acid, a major byproduct, is significantly reduced by employing Corynebacterium glutamicum gabT mutant as a host. Method development and optimization, overview
additional information
Corynebacterium glutamicum KCTC 1857, which naturally producs high amounts of L-lysine, a direct precursor for the production of cadaverine, 5-AVA, and glutaric acid, is metabolically engineered for the production of glutaric acid, a C5 dicarboxylic acid that can be used as platform building block chemical for nylons and plasticizers. Corynebacterium glutamicum gabT and gabD genes and Pseudomonas putida davT and davD genes encoding 5-aminovalerate transaminase and glutarate semialdehyde dehydrogenase, respectively, are examined in Corynebacterium glutamicum for the construction of a glutaric acid biosynthesis pathway along with Pseudomonas putida davB and davA genes encoding lysine 2-monooxygenase and delta-aminovaleramidase, respectively. Evaluation of strong synthetic promoters PH30 and PH36, usage of Corynebacterium glutamicum codon-optimized davTDBA genes, and modification of davB gene with an N-terminal His6-tag are established to improve the production of glutaric acid. N-terminal His6-tagged DavB is most suitable for the production of glutaric acid from glucose. Fed-batch fermentation using the final engineered Corynebacterium glutamicum H30_GAHis strain, expressing davTDA genes along with N-terminally His6-tagged davB produce 24.5 g/l of glutaric acid with low accumulation of L-lysine (1.7 g/l), wherein 5-AVA accumulation is not observed during fermentation
additional information
-
Corynebacterium glutamicum KCTC 1857, which naturally producs high amounts of L-lysine, a direct precursor for the production of cadaverine, 5-AVA, and glutaric acid, is metabolically engineered for the production of glutaric acid, a C5 dicarboxylic acid that can be used as platform building block chemical for nylons and plasticizers. Corynebacterium glutamicum gabT and gabD genes and Pseudomonas putida davT and davD genes encoding 5-aminovalerate transaminase and glutarate semialdehyde dehydrogenase, respectively, are examined in Corynebacterium glutamicum for the construction of a glutaric acid biosynthesis pathway along with Pseudomonas putida davB and davA genes encoding lysine 2-monooxygenase and delta-aminovaleramidase, respectively. Evaluation of strong synthetic promoters PH30 and PH36, usage of Corynebacterium glutamicum codon-optimized davTDBA genes, and modification of davB gene with an N-terminal His6-tag are established to improve the production of glutaric acid. N-terminal His6-tagged DavB is most suitable for the production of glutaric acid from glucose. Fed-batch fermentation using the final engineered Corynebacterium glutamicum H30_GAHis strain, expressing davTDA genes along with N-terminally His6-tagged davB produce 24.5 g/l of glutaric acid with low accumulation of L-lysine (1.7 g/l), wherein 5-AVA accumulation is not observed during fermentation
additional information
lysine 2-monooxygenase (DavB) and delta-aminovaleramidase (DavA) are co-expressed in Escherichia coli BL21(DE3) to produce nylon-5 monomer 5-aminovalerate from L-lysine. Then, PP2911 (4-aminobutyrate transporter in Pseudomonas putida) and LysP (the lysine specific permease in Escherichia coli) are overexpressed to promote 5-aminovalerate production using whole cells of recombinant Escherichia coli, strain optimization for large scale production, overview. Overexpression of transport proteins improves the production of 5-aminovalerate from L-lysine in Escherichia coli. The optimum catalytic conditions are determined to be reaction temperature 30°C, substrate concentration 40 g/l, and biocatalyst concentration 60 OD600nm
additional information
systems metabolic engineering of Corynebacterium glutamicum for construction of a recombinant microbial cell factory for the production of the carbon-5 platform chemicals 5-aminovalerate and glutarate, method development on basis of the lysine-hyperproducing strain Corynebacterium glutamicum LYS-12 and optimization, detailed overview. Related to the presence of endogenous genes coding for 5-aminovalerate transaminase (gabT) and glutarate semialdehyde dehydrogenase, 5-aminovalerate is partially converted to glutarate. Moreover, residual l-lysine is secreted as by-product. The issue of by-product formation is then addressed by deletion of the lysE gene, encoding the l-lysine exporter. Additionally, a putative gabT gene is deleted to enhance 5-aminovalerate production. Fed-batch fermentation. Method optimization, overview. Production of 28 g/l of 5-aminovalerate with a maximal space to time yield of 0.9 g/l per h from engineered AVA-3 strain
additional information
-
systems metabolic engineering of Corynebacterium glutamicum for construction of a recombinant microbial cell factory for the production of the carbon-5 platform chemicals 5-aminovalerate and glutarate, method development on basis of the lysine-hyperproducing strain Corynebacterium glutamicum LYS-12 and optimization, detailed overview. Related to the presence of endogenous genes coding for 5-aminovalerate transaminase (gabT) and glutarate semialdehyde dehydrogenase, 5-aminovalerate is partially converted to glutarate. Moreover, residual l-lysine is secreted as by-product. The issue of by-product formation is then addressed by deletion of the lysE gene, encoding the l-lysine exporter. Additionally, a putative gabT gene is deleted to enhance 5-aminovalerate production. Fed-batch fermentation. Method optimization, overview. Production of 28 g/l of 5-aminovalerate with a maximal space to time yield of 0.9 g/l per h from engineered AVA-3 strain
additional information
-
systems metabolic engineering of Corynebacterium glutamicum for construction of a recombinant microbial cell factory for the production of the carbon-5 platform chemicals 5-aminovalerate and glutarate, method development on basis of the lysine-hyperproducing strain Corynebacterium glutamicum LYS-12 and optimization, detailed overview. Related to the presence of endogenous genes coding for 5-aminovalerate transaminase (gabT) and glutarate semialdehyde dehydrogenase, 5-aminovalerate is partially converted to glutarate. Moreover, residual l-lysine is secreted as by-product. The issue of by-product formation is then addressed by deletion of the lysE gene, encoding the l-lysine exporter. Additionally, a putative gabT gene is deleted to enhance 5-aminovalerate production. Fed-batch fermentation. Method optimization, overview. Production of 28 g/l of 5-aminovalerate with a maximal space to time yield of 0.9 g/l per h from engineered AVA-3 strain
-
additional information
-
combined expression of Pseudomonas putida davB and davA genes encoding lysine 2-monooxygenase and delta-aminovaleramidase, respectively, in engineered Corynebacterium glutamicum strain BE (KCTC 12390BP) for large scale production of 5-aminovalerate (5AVA) under the control of constitutive promoters. Expression of codon-optimized N-terminally His6-tagged davA gene fused the davB gene as an operon under a strong synthetic H36 promoter from plasmid p36davAB3 in Corynebacterium glutamicum in fed-batch culture enables the most efficient production of 5AVA. In addition, production of glutaric acid, a major byproduct, is significantly reduced by employing Corynebacterium glutamicum gabT mutant as a host. Method development and optimization, overview
-
additional information
-
Corynebacterium glutamicum KCTC 1857, which naturally producs high amounts of L-lysine, a direct precursor for the production of cadaverine, 5-AVA, and glutaric acid, is metabolically engineered for the production of glutaric acid, a C5 dicarboxylic acid that can be used as platform building block chemical for nylons and plasticizers. Corynebacterium glutamicum gabT and gabD genes and Pseudomonas putida davT and davD genes encoding 5-aminovalerate transaminase and glutarate semialdehyde dehydrogenase, respectively, are examined in Corynebacterium glutamicum for the construction of a glutaric acid biosynthesis pathway along with Pseudomonas putida davB and davA genes encoding lysine 2-monooxygenase and delta-aminovaleramidase, respectively. Evaluation of strong synthetic promoters PH30 and PH36, usage of Corynebacterium glutamicum codon-optimized davTDBA genes, and modification of davB gene with an N-terminal His6-tag are established to improve the production of glutaric acid. N-terminal His6-tagged DavB is most suitable for the production of glutaric acid from glucose. Fed-batch fermentation using the final engineered Corynebacterium glutamicum H30_GAHis strain, expressing davTDA genes along with N-terminally His6-tagged davB produce 24.5 g/l of glutaric acid with low accumulation of L-lysine (1.7 g/l), wherein 5-AVA accumulation is not observed during fermentation
-
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
EDTA and dithioerythritol required for optimum stability, enzyme stored in their absence rapidly deteriorates
-
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
2-monooxygenase (DavB) and delta-aminovaleramidase (DavA) are coexpressed in Escherichia coli BL21(DE3) to produce nylon-5 monomer 5-aminovalerate from L-lysine
gene davA, coexpression with gene davB from construct pETDuet-DavAB in Escherichia coli strain BL21(DE3)
gene davA, coexpression with Pseudomonas putida genes davB, davT, and davD in Corynebacterium glutamicum engineered strain H30_GAHis under control of strong synthetic promoters PH30 and PH36, fed-batch fermentation
gene davA, functional recombinant expression in Escherichia coli strains WL3110 and XQ56 from vector pKE112-MCS, co-expression with gene davB from Pseudomnas putida, encoding lysine 2-monooxygenase, as well as with gabTD genes encoding 5AVA aminotransferase and glutarate semialdehyde dehydrogenase, addition of L-lysine and 2-oxoglutarate results in synthesis of 5-aminovalerate and glutrate, overview
gene davA, recombinant expression in Corynebacterium glutamicum, coexpression with gene davB from Pseudomonas putida encoding lysine 2-monooxygenase (EC 1.13.12.2)
gene davA, recombinant expression in Corynebacterium glutamicum, coexpression with gene davB from Pseudomonas putida encoding lysine 2-monooxygenase (EC 1.13.12.2)
gene davA, recombinant expression in Corynebacterium glutamicum, coexpression with gene davB from Pseudomonas putida encoding lysine 2-monooxygenase (EC 1.13.12.2)
-
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
synthesis
synthesis
the enzyme is useful to produce the nylon-5 monomer 5-aminovalerate from L-lysine in large scale
synthesis
2-monooxygenase (DavB) and delta-aminovaleramidase (DavA) are coexpressed in Escherichia coli BL21(DE3) to produce nylon-5 monomer 5-aminovalerate from L-lysine. PP2911 (4-aminobutyrate transporter in Pseudomonas putida) and LysP (the lysine specific permease in Escherichia coli) are overexpressed to promote 5-aminovalerate production using whole cells of recombinant Escherichia coli. The constructed Escherichia coli strain overexpressing transport proteins exhibits good 5-aminovalerate production performance and might serve as a promising biocatalyst for 5-aminovalerate production from L-lysine. This strategy not only shows an efficient process for the production of nylon monomers but also might be used in production of other chemicals
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Reitz, M.S.; Rodwell, V.W.
delta-Aminovaleramidase (Pseudomonas putida)
Methods Enzymol.
17
158-165
1971
Pseudomonas putida, Pseudomonas putida P2-ATCC *25571
-
brenda
Reitz, M.S.; Rodwell, V.W.
delta-Aminovaleramidase of Pseudomonas putida
J. Biol. Chem.
245
3091-3096
1970
Pseudomonas putida
brenda
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 (B3IVI7), Pseudomonas putida, Pseudomonas putida ATCC 12633 (B3IVI7)
brenda
Rohles, C.; Giesselmann, G.; Kohlstedt, M.; Wittmann, C.; Becker, J.
Systems metabolic engineering of Corynebacterium glutamicum for the production of the carbon-5 platform chemicals 5-aminovalerate and glutarate
Microb. Cell Fact.
15
154
2016
Pseudomonas putida (B3IVI7), Pseudomonas putida, Pseudomonas putida ATCC 12633 (B3IVI7)
brenda
Shin, J.H.; Park, S.H.; Oh, Y.H.; Choi, J.W.; Lee, M.H.; Cho, J.S.; Jeong, K.J.; Joo, J.C.; Yu, J.; Park, S.J.; Lee, S.Y.
Metabolic engineering of Corynebacterium glutamicum for enhanced production of 5-aminovaleric acid
Microb. Cell Fact.
15
174
2016
Pseudomonas putida (B3IVI7), Pseudomonas putida, Pseudomonas putida ATCC 12633 (B3IVI7)
brenda
Li, Z.; Xu, J.; Jiang, T.; Ge, Y.; Liu, P.; Zhang, M.; Su, Z.; Gao, C.; Ma, C.; Xu, P.
Overexpression of transport proteins improves the production of 5-aminovalerate from L-lysine in Escherichia coli
Sci. Rep.
6
30884
2016
Pseudomonas putida (Q88QV2)
brenda
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
Pseudomonas putida (B3IVI7), Pseudomonas putida, Pseudomonas putida ATCC 12633 (B3IVI7)
brenda
EXTERNAL LINKS (specific for EC-Number 3.5.1.30)
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