DB code: D00269

CATH domain 3.90.1150.10 : Aspartate Aminotransferase, domain 1
3.40.640.10 : Aspartate Aminotransferase; domain 2 Catalytic domain
E.C. 4.4.1.14
CSA 1b8g
M-CSA 1b8g
MACiE

CATH domain Related DB codes (homologues)
3.90.1150.10 : Aspartate Aminotransferase, domain 1 D00085 D00092 D00101 D00102 D00103 D00104 D00107 D00108 D00109 D00255 D00257 D00258 D00265 D00515 M00031 D00279
3.40.640.10 : Aspartate Aminotransferase; domain 2 D00085 D00092 D00101 D00102 D00103 D00104 D00107 D00108 D00109 D00255 D00257 D00258 D00265 D00515 M00031 D00279

Uniprot Enzyme Name
UniprotKB Protein name Synonyms Pfam
P37821 1-aminocyclopropane-1-carboxylate synthase
ACC synthase
EC 4.4.1.14
S-adenosyl-L-methionine methylthioadenosine-lyase
PF00155 (Aminotran_1_2)
[Graphical View]
P18485 1-aminocyclopropane-1-carboxylate synthase 2
ACC synthase 2
EC 4.4.1.14
Le-ACS2
ACS-2
S-adenosyl-L-methionine methylthioadenosine-lyase 2
PF00155 (Aminotran_1_2)
[Graphical View]

KEGG enzyme name
1-aminocyclopropane-1-carboxylate synthase
1-aminocyclopropanecarboxylate synthase
1-aminocyclopropane-1-carboxylic acid synthase
1-aminocyclopropane-1-carboxylate synthetase
aminocyclopropanecarboxylic acid synthase
aminocyclopropanecarboxylate synthase
ACC synthase
S-adenosyl-L-methionine methylthioadenosine-lyase

UniprotKB: Accession Number Entry name Activity Subunit Subcellular location Cofactor
P18485 1A12_SOLLC S-adenosyl-L-methionine = 1-aminocyclopropane- 1-carboxylate + methylthioadenosine. Homodimer and heterodimer. In vivo, the relevance of heterodimerization with other ACS enzymes is however unsure. Pyridoxal phosphate.
P37821 1A1C_MALDO S-adenosyl-L-methionine = 1-aminocyclopropane- 1-carboxylate + methylthioadenosine. Homodimer. Pyridoxal phosphate.

KEGG Pathways
Map code Pathways E.C.
MAP00271 Methionine metabolism

Compound table
Cofactors Substrates Products Intermediates
KEGG-id C00018 C00019 C01234 C00170
E.C.
Compound Pyridoxal phosphate S-Adenosyl-L-methionine 1-Aminocyclopropane-1-carboxylate Methylthioadenosine
Type aromatic ring (with nitrogen atoms),phosphate group/phosphate ion amino acids,amine group,nucleoside,sulfonium ion amino acids amine group,nucleoside,sulfide group
ChEBI 18405
67040
58360
18053
17509
PubChem 1051
34755
6971063
535
439176
1b8gA01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound
1b8gB01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound
1m7yA01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound
1m4nA01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound
1iaxA01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound
1iaxB01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound
1iayA01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound
1b8gA02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Bound:PLP Unbound Unbound Unbound Unbound
1b8gB02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Bound:PLP Unbound Unbound Unbound Unbound
1m7yA02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Analogue:PPG Unbound Unbound Unbound Intermediate-analogue:PPG
1m4nA02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Bound:PLP Analogue:AAD Unbound Unbound Intermediate-analogue:PLP-AAD
1iaxA02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Bound:PLP Unbound Unbound Unbound Unbound
1iaxB02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Bound:PLP Unbound Unbound Unbound Unbound
1iayA02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Bound:PLP Unbound Analogue:AVG Unbound Unbound

Reference for Active-site residues
resource references E.C.
literature [9] & [11]

Active-site residues
PDB Catalytic residues Cofactor-binding residues Modified residues Main-chain involved in catalysis Comment
1b8gA01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain
1b8gB01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain
1m7yA01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain
1m4nA01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain
1iaxA01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain
1iaxB01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain
1iayA01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain
1b8gA02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain TYR 145;LYS 273 LYS 273(PLP binding)
1b8gB02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain TYR 145;LYS 273 LYS 273(PLP binding)
1m7yA02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain TYR 145;LYS 273 LYS 273(PLP binding)
1m4nA02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain TYR 145;LYS 273 LYS 273(PLP binding)
1iaxA02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain TYR 152;LYS 278 LYS 278(PLP binding)
1iaxB02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain TYR 152;LYS 278 LYS 278(PLP binding)
1iayA02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain TYR 152;LYS 278 LYS 278(PLP binding)

References for Catalytic Mechanism
References Sections No. of steps in catalysis
[1]
Fig.4, p.7824
[7]
Scheme 4B, Scheme 6, p.15486-15487
[8]
p.8
[9]
Scheme 2, p.748-749 4
[10]
Scheme 1, Scheme 3A, p.12283 3
[11]
p.38214, Fig.6, p.38215 5
[12]
Scheme 3, p.3840-3841

References
[1]
Resource
Comments
Medline ID
PubMed ID 3865199
Journal Proc Natl Acad Sci U S A
Year 1985
Volume 82
Pages 7820-4
Authors Ramalingam K, Lee KM, Woodard RW, Bleecker AB, Kende H
Title Stereochemical course of the reaction catalyzed by the pyridoxal phosphate-dependent enzyme 1-aminocyclopropane-1-carboxylate synthase.
Related PDB
Related UniProtKB
[2]
Resource
Comments
Medline ID
PubMed ID 2712568
Journal Arch Biochem Biophys
Year 1989
Volume 271
Pages 107-12
Authors Satoh S, Yang SF
Title Specificity of S-adenosyl-L-methionine in the inactivation and the labeling of 1-aminocyclopropane-1-carboxylate synthase isolated from tomato fruits.
Related PDB
Related UniProtKB
[3]
Resource
Comments
Medline ID
PubMed ID 1421146
Journal Plant Mol Biol
Year 1992
Volume 20
Pages 425-36
Authors Botella JR, Arteca JM, Schlagnhaufer CD, Arteca RN, Phillips AT
Title Identification and characterization of a full-length cDNA encoding for an auxin-induced 1-aminocyclopropane-1-carboxylate synthase from etiolated mung bean hypocotyl segments and expression of its mRNA in response to indole-3-acetic acid.
Related PDB
Related UniProtKB
[4]
Resource
Comments
Medline ID
PubMed ID 7966311
Journal J Mol Biol
Year 1994
Volume 243
Pages 947-9
Authors Hohenester E, White MF, Kirsch JF, Jansonius JN
Title Crystallization and preliminary X-ray analysis of recombinant 1-aminocyclopropane-1-carboxylate synthase from apple. A key enzyme in the biosynthesis of the plant hormone ethylene.
Related PDB
Related UniProtKB
[5]
Resource
Comments
Medline ID
PubMed ID 7809054
Journal Proc Natl Acad Sci U S A
Year 1994
Volume 91
Pages 12428-32
Authors White MF, Vasquez J, Yang SF, Kirsch JF
Title Expression of apple 1-aminocyclopropane-1-carboxylate synthase in Escherichia coli: kinetic characterization of wild-type and active-site mutant forms.
Related PDB
Related UniProtKB
[6]
Resource
Comments
Medline ID
PubMed ID 8557119
Journal FEBS Lett
Year 1996
Volume 378
Pages 286-90
Authors Li N, Huxtable S, Yang SF, Kung SD
Title Effects of N-terminal deletions on 1-aminocyclopropane-1-carboxylate synthase activity.
Related PDB
Related UniProtKB
[7]
Resource
Comments
Medline ID
PubMed ID 9398277
Journal Biochemistry
Year 1997
Volume 36
Pages 15477-88
Authors Li Y, Feng L, Kirsch JF
Title Kinetic and spectroscopic investigations of wild-type and mutant forms of apple 1-aminocyclopropane-1-carboxylate synthase.
Related PDB
Related UniProtKB
[8]
Resource
Comments
Medline ID
PubMed ID 9279127
Journal Indian J Exp Biol
Year 1997
Volume 35
Pages 1-17
Authors Penrose DM, Glick BR
Title Enzymes that regulate ethylene levels--1-aminocyclopropane-1-carboxylic acid (ACC) deaminase, ACC synthase and ACC oxidase.
Related PDB
Related UniProtKB
[9]
Resource
Comments X-RAY CRYSTALLOGRAPHY (2.37 ANGSTROMS)
Medline ID 20079531
PubMed ID 10610793
Journal J Mol Biol
Year 1999
Volume 294
Pages 745-56
Authors Capitani G, Hohenester E, Feng L, Storici P, Kirsch JF, Jansonius JN
Title Structure of 1-aminocyclopropane-1-carboxylate synthase, a key enzyme in the biosynthesis of the plant hormone ethylene.
Related PDB 1b8g
Related UniProtKB P37821
[10]
Resource
Comments
Medline ID
PubMed ID 11591146
Journal Biochemistry
Year 2001
Volume 40
Pages 12276-84
Authors McCarthy DL, Capitani G, Feng L, Gruetter MG, Kirsch JF
Title Glutamate 47 in 1-aminocyclopropane-1-carboxylate synthase is a major specificity determinant.
Related PDB
Related UniProtKB
[11]
Resource
Comments X-ray crystallography
Medline ID
PubMed ID 11431475
Journal J Biol Chem
Year 2001
Volume 276
Pages 38210-6
Authors Huai Q, Xia Y, Chen Y, Callahan B, Li N, Ke H
Title Crystal structures of 1-aminocyclopropane-1-carboxylate (ACC) synthase in complex with aminoethoxyvinylglycine and pyridoxal-5'-phosphate provide new insight into catalytic mechanisms.
Related PDB 1iax
Related UniProtKB
[12]
Resource
Comments
Medline ID
PubMed ID 11888303
Journal Biochemistry
Year 2002
Volume 41
Pages 3836-42
Authors Eliot AC, Kirsch JF
Title Modulation of the internal aldimine pK(a)'s of 1-aminocyclopropane-1-carboxylate synthase and aspartate aminotransferase by specific active site residues.
Related PDB
Related UniProtKB
[13]
Resource
Comments
Medline ID
PubMed ID 12228256
Journal J Biol Chem
Year 2002
Volume 277
Pages 49735-42
Authors Capitani G, McCarthy DL, Gut H, Grutter MG, Kirsch JF
Title Apple 1-aminocyclopropane-1-carboxylate synthase in complex with the inhibitor L-aminoethoxyvinylglycine. Evidence for a ketimine intermediate.
Related PDB 1m7y
Related UniProtKB
[14]
Resource
Comments
Medline ID
PubMed ID 12686108
Journal Biochim Biophys Acta
Year 2003
Volume 1647
Pages 55-60
Authors Capitani G, Eliot AC, Gut H, Khomutov RM, Kirsch JF, Grutter MG
Title Structure of 1-aminocyclopropane-1-carboxylate synthase in complex with an amino-oxy analogue of the substrate: implications for substrate binding.
Related PDB 1m4n
Related UniProtKB

Comments
This enzyme catalyzes a PLP-dependent elimination reaction, followed by an isomerization reaction.

Created Updated
2004-05-24 2009-02-26