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Information on EC 3.5.99.7 - 1-aminocyclopropane-1-carboxylate deaminase and Organism(s) Cyberlindnera saturnus and UniProt Accession Q7M523

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EC Tree
IUBMB Comments
A pyridoxal 5'-phosphate enzyme. The enzyme, found in certain soil bacteria and fungi, catalyses the ring opening of 1-aminocyclopropane-1-carboxylate, the immediate precursor to ethylene, an important plant hormone that regulates fruit ripening and other processes. The enzyme releases an unstable enamine product that tautomerizes to an imine form, which undergoes a hydrolytic deamination. The latter reaction, which can occur spontaneously, can also be catalysed by EC 3.5.99.10, 2-iminobutanoate/2-iminopropanoate deaminase. The enzyme has been used to make fruit ripening dependent on externally added ethylene, as it removes the substrate for endogenous ethylene formation.
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This record set is specific for:
Cyberlindnera saturnus
UNIPROT: Q7M523
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The taxonomic range for the selected organisms is: Cyberlindnera saturnus
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Reaction Schemes
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1-aminocyclopropane-1-carboxylate
+
H2O
=
2-oxobutanoate
+
NH3
+
=
+
Synonyms
acc deaminase, 1-aminocyclopropane-1-carboxylate deaminase, acc-deaminase, 1-aminocyclopropane-1-carboxylic acid deaminase, 1-aminocyclopropane-1-carboxylic acid-deaminase, acpc deaminase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
1-aminocyclopropane-1-carboxylate endolyase (deaminating)
-
-
-
-
1-aminocyclopropane-1-carboxylic acid deaminase
-
-
-
-
ACC deaminase
ACPC deaminase
-
-
-
-
deaminase, 1-aminocyclopropane-1-carboxylate
-
-
-
-
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
1-aminocyclopropane-1-carboxylate + H2O = 2-oxobutanoate + NH3
show the reaction diagram
mechanism
1-aminocyclopropane-1-carboxylate + H2O = 2-oxobutanoate + NH3
show the reaction diagram
mechanism
-
PATHWAY SOURCE
PATHWAYS
SYSTEMATIC NAME
IUBMB Comments
1-aminocyclopropane-1-carboxylate aminohydrolase (isomerizing)
A pyridoxal 5'-phosphate enzyme. The enzyme, found in certain soil bacteria and fungi, catalyses the ring opening of 1-aminocyclopropane-1-carboxylate, the immediate precursor to ethylene, an important plant hormone that regulates fruit ripening and other processes. The enzyme releases an unstable enamine product that tautomerizes to an imine form, which undergoes a hydrolytic deamination. The latter reaction, which can occur spontaneously, can also be catalysed by EC 3.5.99.10, 2-iminobutanoate/2-iminopropanoate deaminase. The enzyme has been used to make fruit ripening dependent on externally added ethylene, as it removes the substrate for endogenous ethylene formation.
CAS REGISTRY NUMBER
COMMENTARY hide
69553-48-6
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
1-aminocyclopropane-1-carboxylate + H2O
2-oxobutanoate + NH3
show the reaction diagram
coronamic acid + H2O
2-oxobutanoate + NH3
show the reaction diagram
-
DL-coronamic acid
-
-
?
D-cystine + H2O
?
show the reaction diagram
-
-
-
-
?
D-Ser + H2O
?
show the reaction diagram
-
-
-
-
?
D-serine + H2O
?
show the reaction diagram
-
-
-
-
?
DL-coronamic acid + H2O
?
show the reaction diagram
-
-
-
-
?
additional information
?
-
-
beta-chloro-D-alanine and O-acetyl-D-serine are not a functional substrate
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
1-aminocyclopropane-1-carboxylate + H2O
2-oxobutanoate + NH3
show the reaction diagram
-
-
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
pyridoxal 5'-phosphate
-
-
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
L-2-aminobutanoate
-
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2.6
1-aminocyclopropane-1-carboxylate
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
-
-
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
1A1D_CYBSA
341
0
37061
Swiss-Prot
Mitochondrion (Reliability: 4)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
40000
-
2 * 40000, SDS-PAGE
69000
-
gel filtration, disc gel electrophoresis
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dimer
-
2 * 40000, SDS-PAGE
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
mutants K51T and Y295F in complex with substrate
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
K51T
crystal structure in complex with substrate
Y295F
crystal structure in complex with substrate
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
subcloned into pET-11d and expressed in Escherichia coli
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
agriculture
-
ability of transgenic tomato plants expressing the enzyme under different promoters to grow in the presence of metal ions
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Honma, M.; Shimomura, T.
Metabolism of 1-aminocyclopropane-1-carboxylic acid
Agric. Biol. Chem.
42
1825-1831
1978
Cyberlindnera saturnus, Pseudomonas sp.
-
Manually annotated by BRENDA team
Yao, M.; Horiuchi, A.; Tanaka, I.; Honma, M.
Crystallization of 1-aminocyclopropane-1-carboxylic acid deaminase from yeast
Protein Pept. Lett.
2
305-306
1995
Cyberlindnera saturnus
-
Manually annotated by BRENDA team
Minami, R.; Uchiyama, K.; Murakami, T.; Kawai, J.; Mikami, K.; Yamada, T.; Yokoi, D.; Ito, H.; Matsui, H.; Honma, M.
Properties, sequence, and synthesis in Escherichia coli of 1-aminocyclopropane-1-carboxylate deaminase from Hansenula saturnus
J. Biochem.
123
1112-1118
1998
Cyberlindnera saturnus
Manually annotated by BRENDA team
Yao, M.; Ose, T.; Sugimoto, H.; Horiuchi, A.; Nakagawa, A.; Wakatsuki, S.; Yokoi, D.; Murakami, T.; Honma, M.; Tanaka, I.
Crystal structure of 1-aminocyclopropane-1-carboxylate deaminase from Hansenula saturnus
J. Biol. Chem.
275
34557-34565
2000
Cyberlindnera saturnus
Manually annotated by BRENDA team
Ose, T.; Fujino, A.; Yao, M.; Watanabe, N.; Honma, M.; Tanaka, I.
Reaction intermediate structures of 1-aminocyclopropane-1-carboxylate deaminase: insight into PLP-dependent cyclopropane ring-opening reaction
J. Biol. Chem.
278
41069-41076
2003
Cyberlindnera saturnus (Q7M523)
Manually annotated by BRENDA team
Grichko, V.P.; Filby, B.; Glick, B.R.
Increased ability of transgenic plants expressing the bacterial enzyme ACC deaminase to accumulate Cd, Co, Cu, Ni, Pb, and Zn
J. Biotechnol.
81
45-53
2000
Enterobacter cloacae, Cyberlindnera saturnus, Enterobacter cloacae UW4
Manually annotated by BRENDA team
Nascimento, F.; Rossi, M.; Soares, C.; McConkey, B.; Glick, B.
New insights into 1-aminocyclopropane-1-carboxylate (ACC) deaminase phylogeny, evolution and ecological significance
PLoS ONE
9
e99168
2014
Arabidopsis thaliana, Cyberlindnera saturnus, Penicillium citrinum, Pseudomonas sp., Methylobacterium radiotolerans, Methylobacterium nodulans, Pseudomonas putida (Q5PWZ8), Bradyrhizobium japonicum (Q89XR6), Bradyrhizobium japonicum USDA 110 (Q89XR6), Pseudomonas putida UW4 (Q5PWZ8)
Manually annotated by BRENDA team