6.3.2.26: N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase

This is an abbreviated version!
For detailed information about N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase, go to the full flat file.

Reaction

3 ATP +

Synonyms

ACV synthetase, ACVS, DELTA-(alpha-aminoadipyl)cysteinylvaline synthetase, delta-(L-alpha-aminoadipoyl)-L-cysteinyl-D-valine synthetase, delta-(L-alpha-aminoadipyl)-L-cysteinyl-D-valine synthetase, delta-(L-alpha-aminoadipyl-L-cysteinyl-D-valine synthetase), delta-L-(alpha-aminoadipyl)-L-cysteinyl-D-valine synthetase, L-(alpha-aminoadipyl)-L-cysteinyl-D-valine synthetase, L-delta-(alpha-aminoadipoyl)-L-cysteinyl-D-valine synthetase, L-delta-alpha-aminoadipoyl-L-cysteinyl-D-valine synthetase, phosphopantothenate synthetase, Pps, synthetase, delta-(alpha-aminoadipyl)cysteinylvaline, TK1686

ECTree

     6 Ligases

         6.3 Forming carbon-nitrogen bonds

             6.3.2 Acid—amino-acid ligases (peptide synthases)

                6.3.2.26 N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase

Advanced search results

Do not include text mining results

Include results (more...)

Include results (more...)

Results	in table
76	AA Sequence
2	Application
1	CAS Registry Number
8	Cloned(Commentary)
17	Cofactor
7	General Information
1	General Stability
23	Inhibitors
12	KM Value [mM]
2	Localization
10	Metals/Ions
14	Molecular Weight [Da]
8	Natural Substrates/ Products (Substrates)
2	Organic Solvent Stability
35	Organism
4	Pathway
8	PDB ID
5	pH Optimum
2	pH Range
2	pH Stability
1	Posttranslational Modification
2	Protein Variants
8	Purification (Commentary)
1	Reaction
3	Reaction Type
33	Reference
1	Source Tissue
5	Specific Activity [micromol/min/mg]
3	Storage Stability
50	Substrates and Products (Substrate)
6	Subunits
25	Synonyms
1	Systematic Name
4	Temperature Optimum [°C]
2	Temperature Range [°C]
11	Temperature Stability [°C]
2	Turnover Number [1/s]

Natural Substrates Products

print visible entries

print all entries

Go back to the abbreviated version
of the Enzyme Summary Page.

Natural Substrates Products on EC 6.3.2.26 - N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase

Please wait a moment until all data is loaded. This message will disappear when all data is loaded.

top print hide show all columns Go to Natural Substrate Search

Please wait a moment until the data is sorted. This message will disappear when the data is sorted.

NATURAL SUBSTRATE

NATURAL PRODUCT

REACTION DIAGRAM

ORGANISM

UNIPROT

COMMENTARY
(Substrate)

LITERATURE
(Substrate)

COMMENTARY
(Product)

LITERATURE
(Product)

REVERSIBILITY
r=reversible
ir=irreversible
?=not specified

3 ATP + L-2-aminohexanedioate + L-cysteine + L-valine + H2O

3 AMP + 3 diphosphate + N-[L-5-amino-5-carboxypentanoyl]-L-cysteinyl-D-valine

3 entries

alpha-aminoadipic acid + L-valine + L-lysine + ?

L-delta-alpha-aminoadipyl-L-cysteinyl-D-valine + ?

Actinomyces sp.

-

enzyme is a nonribosomal peptide synthetase (NRPS) able to form ribosome-independent peptide bonds

700004

ACV

-

?

ATP + (R)-4-phosphopantoate + beta-alanine

AMP + diphosphate + (R)-4'-phosphopantothenate

Thermococcus kodakarensis

Q5JIZ8

the enzyme is involved in coenzyme A biosynthesis in the archaea

727436

-

-

?

additional information

?

-

2 entries

3 ATP + L-2-aminohexanedioate + L-cysteine + L-valine + H2O

3 AMP + 3 diphosphate + N-[L-5-amino-5-carboxypentanoyl]-L-cysteinyl-D-valine

Penicillium chrysogenum

B6HLU1

-

726783, 727108

-

-

?

3 ATP + L-2-aminohexanedioate + L-cysteine + L-valine + H2O

3 AMP + 3 diphosphate + N-[L-5-amino-5-carboxypentanoyl]-L-cysteinyl-D-valine

Penicillium chrysogenum

-

-

727108

-

-

?

3 ATP + L-2-aminohexanedioate + L-cysteine + L-valine + H2O

3 AMP + 3 diphosphate + N-[L-5-amino-5-carboxypentanoyl]-L-cysteinyl-D-valine

Penicillium chrysogenum Wisconsin 54-1255

B6HLU1

-

726783, 727108

-

-

?

additional information

?

-

Actinomyces sp.

-

ACVSs are multifunctional enzymes that activate amino acids as aminoacyladenylates, forming a mixed anhydride with the a-phosphate group of ATP and releasing pyrophosphate

700004

-

-

?

additional information

?

-

Actinomyces sp.

-

pure Streptomyces lactamdurans ACVS is able to activate alpha-aminoadipic acid or its lactam 6-oxopiperideine-2-carboxylic acid, a compound that is easily converted to alpha-aminoadipic acid, but is unable to use piperideine-6-carboxylate or pipecolic acid as substrates, enzyme is also able to use L-cystathionine with the same efficiency as L-cysteine

700004

-

-

?