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Methylaspartate ammonia-lyase (MAL) (EC 4.3.1.2) (3-methylaspartase ammonia-lyase) (Beta-methylaspartase)

 MAAL_CLOTT              Reviewed;         413 AA.
Q05514;
01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
01-FEB-1995, sequence version 1.
05-DEC-2018, entry version 94.
RecName: Full=Methylaspartate ammonia-lyase;
Short=MAL;
EC=4.3.1.2;
AltName: Full=3-methylaspartase ammonia-lyase;
AltName: Full=Beta-methylaspartase;
Clostridium tetanomorphum.
Bacteria; Firmicutes; Clostridia; Clostridiales; Clostridiaceae;
Clostridium.
NCBI_TaxID=1553;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-26, FUNCTION,
CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND SUBUNIT.
STRAIN=ATCC 15920 / DSM 528 / NCIMB 11547 / H1;
PubMed=1420191; DOI=10.1021/bi00159a015;
Goda S.K., Minton N.P., Botting N.P., Gani D.;
"Cloning, sequencing, and expression in Escherichia coli of the
Clostridium tetanomorphum gene encoding beta-methylaspartase and
characterization of the recombinant protein.";
Biochemistry 31:10747-10756(1992).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-24, AND PROTEIN SEQUENCE OF
1-24.
STRAIN=ATCC 15920 / DSM 528 / NCIMB 11547 / H1;
PubMed=8454064; DOI=10.1016/0014-5793(93)80042-S;
Brecht M., Kellermann J., Plueckthun A.;
"Cloning and sequencing of glutamate mutase component E from
Clostridium tetanomorphum.";
FEBS Lett. 319:84-89(1993).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-71.
STRAIN=ATCC 15920 / DSM 528 / NCIMB 11547 / H1;
PubMed=8428631; DOI=10.1016/0014-5793(93)81488-L;
Holloway D.E., Marsh E.N.G.;
"Cloning and sequencing of glutamate mutase component E from
Clostridium tetanomorphum. Organization of the mut genes.";
FEBS Lett. 317:44-48(1993).
[4]
PROTEIN SEQUENCE OF 1-15.
STRAIN=ATCC 15920 / DSM 528 / NCIMB 11547 / H1;
PubMed=1397267; DOI=10.1016/0014-5793(92)81321-C;
Marsh E.N.G., Holloway D.E.;
"Cloning and sequencing of glutamate mutase component S from
Clostridium tetanomorphum. Homologies with other cobalamin-dependent
enzymes.";
FEBS Lett. 310:167-170(1992).
[5]
FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, ACTIVITY
REGULATION, SUBSTRATE SPECIFICITY, AND COFACTOR.
STRAIN=ATCC 15920 / DSM 528 / NCIMB 11547 / H1;
PubMed=13630903;
Barker H.A., Smyth R.D., Wilson R.M., Weissbach H.;
"The purification and properties of beta-methylaspartase.";
J. Biol. Chem. 234:320-328(1959).
[6]
FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES,
MUTAGENESIS OF HIS-194; GLN-329 AND LYS-331, SUBSTRATE SPECIFICITY,
ACTIVE SITE, AND SUBUNIT.
STRAIN=ATCC 15920 / DSM 528 / NCIMB 11547 / H1;
PubMed=19670200; DOI=10.1002/cbic.200900311;
Raj H., Weiner B., Veetil V.P., Reis C.R., Quax W.J., Janssen D.B.,
Feringa B.L., Poelarends G.J.;
"Alteration of the diastereoselectivity of 3-methylaspartate ammonia
lyase by using structure-based mutagenesis.";
ChemBioChem 10:2236-2245(2009).
[7]
X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) IN COMPLEX WITH MAGNESIUM,
ACTIVE SITE, COFACTOR, AND SUBUNIT.
PubMed=11748244; DOI=10.1074/jbc.M111180200;
Asuncion M., Blankenfeldt W., Barlow J.N., Gani D., Naismith J.H.;
"The structure of 3-methylaspartase from Clostridium tetanomorphum
functions via the common enolase chemical step.";
J. Biol. Chem. 277:8306-8311(2002).
[8]
X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) IN COMPLEX WITH SUBSTRATE
ANALOGS AND MAGNESIUM, FUNCTION, CATALYTIC ACTIVITY, MUTAGENESIS OF
GLN-73 AND LEU-384, COFACTOR, AND SUBUNIT.
PubMed=22614383; DOI=10.1038/nchem.1338;
Raj H., Szymanski W., de Villiers J., Rozeboom H.J., Veetil V.P.,
Reis C.R., de Villiers M., Dekker F.J., de Wildeman S., Quax W.J.,
Thunnissen A.M., Feringa B.L., Janssen D.B., Poelarends G.J.;
"Engineering methylaspartate ammonia lyase for the asymmetric
synthesis of unnatural amino acids.";
Nat. Chem. 4:478-484(2012).
-!- FUNCTION: Involved in the methylaspartate cycle. Catalyzes the
formation of the alpha,beta-unsaturated bond by the reversible
anti elimination of ammonia from L-threo-beta-methylaspartate (L-
threo-(2S,3S)-3-methylaspartate) to give mesaconate. It can also
use L-erythro-beta-methylaspartate (L-erythro-(2S,3R)-3-
methylaspartate), L-aspartate, fumarate and ethylfumarate as
substrates. {ECO:0000269|PubMed:13630903,
ECO:0000269|PubMed:1420191, ECO:0000269|PubMed:19670200,
ECO:0000269|PubMed:22614383}.
-!- CATALYTIC ACTIVITY:
Reaction=(2S,3S)-3-methyl-L-aspartate = mesaconate + NH4(+);
Xref=Rhea:RHEA:12829, ChEBI:CHEBI:28938, ChEBI:CHEBI:36986,
ChEBI:CHEBI:58724; EC=4.3.1.2;
Evidence={ECO:0000269|PubMed:13630903,
ECO:0000269|PubMed:1420191, ECO:0000269|PubMed:19670200,
ECO:0000269|PubMed:22614383};
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
Evidence={ECO:0000269|PubMed:11748244,
ECO:0000269|PubMed:13630903, ECO:0000269|PubMed:22614383};
-!- ACTIVITY REGULATION: Inhibited by calcium ions.
{ECO:0000269|PubMed:13630903}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=0.65 mM for L-threo-beta-methylaspartate (with 4 mM of KCl at
pH 9.76 and at 25 degrees Celsius) {ECO:0000269|PubMed:13630903,
ECO:0000269|PubMed:1420191, ECO:0000269|PubMed:19670200};
KM=0.67 mM for L-threo-beta-methylaspartate (with 50 mM of KCl
at pH 9 and at 30 degrees Celsius) {ECO:0000269|PubMed:13630903,
ECO:0000269|PubMed:1420191, ECO:0000269|PubMed:19670200};
KM=0.7 mM for mesaconate (with 20 mM of MgCl(2) at pH 9 and at
30 degrees Celsius) {ECO:0000269|PubMed:13630903,
ECO:0000269|PubMed:1420191, ECO:0000269|PubMed:19670200};
KM=1 mM for L-threo-beta-methylaspartate (with 20 mM of MgCl(2)
at pH 9 and at 30 degrees Celsius) {ECO:0000269|PubMed:13630903,
ECO:0000269|PubMed:1420191, ECO:0000269|PubMed:19670200};
KM=2.3 mM for L-aspartate (with 4 mM of KCl at pH 9.76 and at 25
degrees Celsius) {ECO:0000269|PubMed:13630903,
ECO:0000269|PubMed:1420191, ECO:0000269|PubMed:19670200};
KM=2.8 mM for L-threo-beta-methylaspartate (with 0.3 mM of KCl
at pH 9 and at 30 degrees Celsius) {ECO:0000269|PubMed:13630903,
ECO:0000269|PubMed:1420191, ECO:0000269|PubMed:19670200};
Vmax=2089 umol/min/mg enzyme with L-threo-beta-methylaspartate
as substrate (with 50 mM of KCl at pH 9 and at 30 degrees
Celsius) {ECO:0000269|PubMed:13630903,
ECO:0000269|PubMed:1420191, ECO:0000269|PubMed:19670200};
Vmax=309 umol/min/mg enzyme with L-threo-beta-methylaspartate as
substrate (with 0.3 mM of KCl at pH 9 and at 30 degrees Celsius)
{ECO:0000269|PubMed:13630903, ECO:0000269|PubMed:1420191,
ECO:0000269|PubMed:19670200};
Vmax=266 umol/min/mg enzyme with L-threo-beta-methylaspartate as
substrate (with 4 mM of KCl at pH 9.76 and at 25 degrees
Celsius) {ECO:0000269|PubMed:13630903,
ECO:0000269|PubMed:1420191, ECO:0000269|PubMed:19670200};
Vmax=2.5 umol/min/mg enzyme with L-erythro-beta-methylaspartate
as substrate (with 4 mM of KCl at pH 9.76 and at 25 degrees
Celsius) {ECO:0000269|PubMed:13630903,
ECO:0000269|PubMed:1420191, ECO:0000269|PubMed:19670200};
Vmax=2.4 umol/min/mg enzyme with L-aspartate as substrate (with
4 mM of KCl at pH 9.76 and at 25 degrees Celsius)
{ECO:0000269|PubMed:13630903, ECO:0000269|PubMed:1420191,
ECO:0000269|PubMed:19670200};
Note=Kcat is 61 sec(-1) for amination of mesaconate (with 20 mM
of MgCl(2) at pH 9 and at 30 degrees Celsius). Kcat is 89 sec(-
1) for deamination of L-threo-beta-methylaspartate (with 20 mM
of MgCl(2) at pH 9 and at 30 degrees Celsius).;
pH dependence:
Optimum pH is 9.7. {ECO:0000269|PubMed:13630903,
ECO:0000269|PubMed:1420191, ECO:0000269|PubMed:19670200};
Temperature dependence:
Optimum temperature is 55 degrees Celsius. It retains only half
of its original activity after a 30 minutes incubation period at
50 degrees Celsius. {ECO:0000269|PubMed:13630903,
ECO:0000269|PubMed:1420191, ECO:0000269|PubMed:19670200};
-!- PATHWAY: Amino-acid degradation; L-glutamate degradation via
mesaconate pathway; acetate and pyruvate from L-glutamate: step
2/4.
-!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:11748244,
ECO:0000269|PubMed:1420191, ECO:0000269|PubMed:19670200,
ECO:0000269|PubMed:22614383}.
-!- SIMILARITY: Belongs to the methylaspartate ammonia-lyase family.
{ECO:0000305}.
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EMBL; S48141; AAB24070.1; -; Genomic_DNA.
EMBL; X70499; CAA49911.1; -; Genomic_DNA.
EMBL; X70695; CAA50027.1; -; Genomic_DNA.
PIR; B44285; B44285.
PDB; 1KCZ; X-ray; 1.90 A; A/B=1-413.
PDB; 1KD0; X-ray; 1.90 A; A/B=1-413.
PDB; 3ZVH; X-ray; 1.99 A; A/B=1-413.
PDB; 3ZVI; X-ray; 1.90 A; A/B=1-413.
PDBsum; 1KCZ; -.
PDBsum; 1KD0; -.
PDBsum; 3ZVH; -.
PDBsum; 3ZVI; -.
ProteinModelPortal; Q05514; -.
SMR; Q05514; -.
DrugBank; DB03661; Cysteinesulfonic Acid.
PRIDE; Q05514; -.
BioCyc; MetaCyc:MONOMER-1103; -.
BRENDA; 4.3.1.2; 1527.
UniPathway; UPA00561; UER00618.
EvolutionaryTrace; Q05514; -.
GO; GO:0031419; F:cobalamin binding; IEA:UniProtKB-KW.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0050096; F:methylaspartate ammonia-lyase activity; IEA:UniProtKB-EC.
GO; GO:0019553; P:glutamate catabolic process via L-citramalate; IEA:UniProtKB-UniPathway.
CDD; cd03314; MAL; 1.
Gene3D; 3.20.20.120; -; 1.
Gene3D; 3.30.390.10; -; 1.
InterPro; IPR036849; Enolase-like_C_sf.
InterPro; IPR029017; Enolase-like_N.
InterPro; IPR006395; Me_Asp_am_lyase.
InterPro; IPR022662; MeAsp_NH4-lyase_C.
InterPro; IPR022665; MeAsp_NH4-lyase_N.
Pfam; PF07476; MAAL_C; 1.
Pfam; PF05034; MAAL_N; 1.
PIRSF; PIRSF017107; MAL; 1.
SFLD; SFLDG00151; methylaspartate_ammonia-lyase; 1.
SUPFAM; SSF51604; SSF51604; 1.
TIGRFAMs; TIGR01502; B_methylAsp_ase; 1.
1: Evidence at protein level;
3D-structure; Cobalamin; Cobalt; Direct protein sequencing; Lyase;
Magnesium; Metal-binding.
CHAIN 1 413 Methylaspartate ammonia-lyase.
/FTId=PRO_0000084547.
REGION 360 361 L-threo-beta-methylaspartate binding.
{ECO:0000250}.
ACT_SITE 331 331 Proton acceptor.
{ECO:0000269|PubMed:11748244,
ECO:0000269|PubMed:19670200}.
METAL 238 238 Magnesium. {ECO:0000269|PubMed:11748244,
ECO:0000269|PubMed:22614383}.
METAL 273 273 Magnesium. {ECO:0000269|PubMed:11748244,
ECO:0000269|PubMed:22614383}.
METAL 307 307 Magnesium. {ECO:0000269|PubMed:11748244,
ECO:0000269|PubMed:22614383}.
BINDING 172 172 L-threo-beta-methylaspartate.
{ECO:0000250}.
BINDING 329 329 L-threo-beta-methylaspartate.
BINDING 361 361 L-threo-beta-methylaspartate.
SITE 194 194 Transition state stabilizer.
MUTAGEN 73 73 Q->A: It has very broad nucleophile scope
and excellent regio- and
diastereoselectivity in the amination
reaction. This mutation strongly moves
the specificity of MAL away from ammonia
and towards methylamine. It is highly
enantioselective.
{ECO:0000269|PubMed:22614383}.
MUTAGEN 194 194 H->A: Strong (160-fold) decrease of the
catalytic efficiency for deamination and
slight (1.8-fold) decrease of affinity
binding for L-threo-beta-methylaspartate.
7-fold decrease of the catalytic
efficiency for amination and 20-fold
decrease of affinity binding for
mesaconate. It does not show any major
conformational changes.
{ECO:0000269|PubMed:19670200}.
MUTAGEN 194 194 H->R: It abolishes deaminase and aminase
activities and does not show any major
conformational changes.
{ECO:0000269|PubMed:19670200}.
MUTAGEN 329 329 Q->A: Very strong decrease of the
catalytic efficiency for deamination,
whereas the affinity binding for L-threo-
beta-methylaspartate is not affected.
Strong (240-fold) decrease of the
catalytic efficiency for amination and
slight (2.4-fold) decrease of affinity
binding for mesaconate. It does not show
any major conformational changes.
{ECO:0000269|PubMed:19670200}.
MUTAGEN 329 329 Q->R: It abolishes deaminase and aminase
activities and does not show any major
conformational changes.
{ECO:0000269|PubMed:19670200}.
MUTAGEN 331 331 K->A: It abolishes deaminase and aminase
activities and does not show any major
conformational changes.
{ECO:0000269|PubMed:19670200}.
MUTAGEN 331 331 K->G: It abolishes deaminase and aminase
activities and does not show any major
conformational changes.
{ECO:0000269|PubMed:19670200}.
MUTAGEN 331 331 K->H: It abolishes deaminase and aminase
activities and does not show any major
conformational changes.
{ECO:0000269|PubMed:19670200}.
MUTAGEN 331 331 K->Q: It abolishes deaminase and aminase
activities and does not show any major
conformational changes.
{ECO:0000269|PubMed:19670200}.
MUTAGEN 331 331 K->R: It abolishes deaminase and aminase
activities and does not show any major
conformational changes.
{ECO:0000269|PubMed:19670200}.
MUTAGEN 384 384 L->A: It has very broad electrophile
scope and excellent regio- and
enantioselectivity in the amination
reaction. {ECO:0000269|PubMed:22614383}.
STRAND 2 11 {ECO:0000244|PDB:1KCZ}.
STRAND 14 18 {ECO:0000244|PDB:1KCZ}.
HELIX 20 24 {ECO:0000244|PDB:1KCZ}.
STRAND 28 30 {ECO:0000244|PDB:1KCZ}.
STRAND 33 36 {ECO:0000244|PDB:1KCZ}.
STRAND 44 49 {ECO:0000244|PDB:1KCZ}.
STRAND 52 59 {ECO:0000244|PDB:1KCZ}.
STRAND 64 69 {ECO:0000244|PDB:1KCZ}.
TURN 73 76 {ECO:0000244|PDB:1KCZ}.
HELIX 86 96 {ECO:0000244|PDB:1KCZ}.
HELIX 98 101 {ECO:0000244|PDB:1KCZ}.
HELIX 109 118 {ECO:0000244|PDB:1KCZ}.
HELIX 128 146 {ECO:0000244|PDB:1KCZ}.
HELIX 150 158 {ECO:0000244|PDB:1KCZ}.
HELIX 179 186 {ECO:0000244|PDB:1KCZ}.
STRAND 190 194 {ECO:0000244|PDB:1KCZ}.
HELIX 200 204 {ECO:0000244|PDB:1KCZ}.
HELIX 209 225 {ECO:0000244|PDB:1KCZ}.
STRAND 234 238 {ECO:0000244|PDB:1KCZ}.
HELIX 242 246 {ECO:0000244|PDB:1KCZ}.
TURN 247 249 {ECO:0000244|PDB:1KCZ}.
HELIX 251 265 {ECO:0000244|PDB:1KCZ}.
STRAND 270 273 {ECO:0000244|PDB:1KCZ}.
HELIX 281 298 {ECO:0000244|PDB:1KCZ}.
STRAND 302 306 {ECO:0000244|PDB:1KCZ}.
HELIX 313 321 {ECO:0000244|PDB:1KCZ}.
STRAND 325 330 {ECO:0000244|PDB:1KCZ}.
HELIX 333 335 {ECO:0000244|PDB:1KCZ}.
HELIX 339 350 {ECO:0000244|PDB:1KCZ}.
STRAND 354 357 {ECO:0000244|PDB:1KCZ}.
HELIX 365 378 {ECO:0000244|PDB:1KCZ}.
STRAND 381 384 {ECO:0000244|PDB:1KCZ}.
STRAND 387 391 {ECO:0000244|PDB:1KCZ}.
HELIX 392 410 {ECO:0000244|PDB:1KCZ}.
SEQUENCE 413 AA; 45534 MW; 4451923DB035EF13 CRC64;
MKIVDVLCTP GLTGFYFDDQ RAIKKGAGHD GFTYTGSTVT EGFTQVRQKG ESISVLLVLE
DGQVAHGDCA AVQYSGAGGR DPLFLAKDFI PVIEKEIAPK LIGREITNFK PMAEEFDKMT
VNGNRLHTAI RYGITQAILD AVAKTRKVTM AEVIRDEYNP GAEINAVPVF AQSGDDRYDN
VDKMIIKEAD VLPHALINNV EEKLGLKGEK LLEYVKWLRD RIIKLRVRED YAPIFHIDVY
GTIGAAFDVD IKAMADYIQT LAEAAKPFHL RIEGPMDVED RQKQMEAMRD LRAELDGRGV
DAELVADEWC NTVEDVKFFT DNKAGHMVQI KTPDLGGVNN IADAIMYCKA NGMGAYCGGT
CNETNRSAEV TTNIGMACGA RQVLAKPGMG VDEGMMIVKN EMNRVLALVG RRK


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Pathways :
WP668: Octadecanoid Pathway
WP1030: Selenium metabolism Selenoproteins
WP108: Selenium metabolism/Selenoproteins
WP1149: Selenium metabolism Selenoproteins
WP1293: Selenium metabolism Selenoproteins
WP1358: Selenium metabolism Selenoproteins
WP1640: Cysteine and methionine metabolism
WP1700: Selenoamino acid metabolism
WP1705: Sulfur metabolism
WP1718: Vitamin B6 metabolism
WP28: Selenium Metabolism and Selenoproteins
WP390: Serine-isocitrate lyase pathway
WP1045: TGF-beta Receptor Signaling Pathway
WP1048: TGF Beta Signaling Pathway
WP105: Fatty Acid Beta Oxidation 2
WP1058: Senescence and Autophagy
WP1061: Fatty Acid Beta Oxidation
WP1106: Keap1-Nrf2
WP1107: Mitochondrial LC-Fatty Acid Beta-Oxidation
WP113: TGF Beta Signaling Pathway
WP1161: TGF-beta Receptor Signaling Pathway
WP1164: TGF Beta Signaling Pathway
WP1177: Fatty Acid Beta Oxidation
WP1207: Fatty Acid Beta Oxidation
WP1224: EBV LMP1 signaling

Related Genes :
[ygeX b2871 JW2839] Diaminopropionate ammonia-lyase (DAPAL) (EC 4.3.1.15) (2,3-diaminopropionate ammonia-lyase) (Alpha,beta-diaminopropionate ammonia-lyase) (Diaminopropionatase)
[srr DDB_G0289463] Probable serine racemase (EC 4.3.1.17) (EC 4.3.1.18) (EC 5.1.1.18) (D-serine ammonia-lyase) (D-serine dehydratase) (L-serine ammonia-lyase) (L-serine dehydratase)
[mcl1 RHOS4_03500 RSP_1771] L-malyl-CoA/beta-methylmalyl-CoA lyase (EC 4.1.3.24) ((3S)-malyl-CoA/beta-methylmalyl-CoA lyase) ((S)-citramalyl-CoA lyase) (EC 4.1.3.25)
[Srr] Serine racemase (EC 5.1.1.18) (D-serine ammonia-lyase) (D-serine dehydratase) (EC 4.3.1.18) (L-serine ammonia-lyase) (L-serine dehydratase) (EC 4.3.1.17)
[SRR] Serine racemase (EC 5.1.1.18) (D-serine ammonia-lyase) (D-serine dehydratase) (EC 4.3.1.18) (L-serine ammonia-lyase) (L-serine dehydratase) (EC 4.3.1.17)
[Srr] Serine racemase (EC 5.1.1.18) (D-serine ammonia-lyase) (D-serine dehydratase) (EC 4.3.1.18) (L-serine ammonia-lyase) (L-serine dehydratase) (EC 4.3.1.17)
[SERR Os04g0555900 LOC_Os04g46930 OsJ_15733 OSJNBb0012E24.7] Serine racemase (EC 4.3.1.17) (EC 4.3.1.18) (EC 5.1.1.18) (D-serine ammonia-lyase) (D-serine dehydratase) (L-serine ammonia-lyase) (L-serine dehydratase)
[SRR] Serine racemase (EC 4.3.1.17) (EC 4.3.1.18) (EC 5.1.1.18) (D-serine ammonia-lyase) (D-serine dehydratase) (L-serine ammonia-lyase) (L-serine dehydratase)
[cmdF] Tyrosine 2,3-aminomutase (EC 5.4.3.6) (Tyrosine ammonia-lyase) (EC 4.3.1.23)
[Smlt1473] Polysaccharide lyase (PL) (EC 4.2.2.-) (Alginate lyase) (EC 4.2.2.3) (Endolytic polysaccharide lyase) (Hyaluronate lyase) (EC 4.2.2.1) (Multifunctional polysaccharide lyase) (Poly-beta-D-glucuronate lyase) (EC 4.2.2.14)
[mcl] Malyl-CoA/beta-methylmalyl-CoA/citramalyl-CoA lyase (EC 4.1.3.24) (EC 4.1.3.25) ((3S)-3-carboxy-3-hydroxypropanoyl-CoA glyoxylate-lyase) ((3S)-citramalyl-CoA pyruvate-lyase) ((S)-citramalyl-CoA lyase) (Erythro-beta-methylmalyl-CoA) (L-malyl-CoA lyase)
[SRY1 YKL218C] L-threo-3-hydroxyaspartate ammonia-lyase (EC 4.3.1.16) (L-threo-3-hydroxyaspartate dehydratase)
[Ogg1] N-glycosylase/DNA lyase [Includes: 8-oxoguanine DNA glycosylase (EC 3.2.2.-); DNA-(apurinic or apyrimidinic site) lyase (AP lyase) (EC 4.2.99.18)]
[thadh] L-threo-3-hydroxyaspartate ammonia-lyase (EC 4.3.1.16) (L-threo-3-hydroxyaspartate dehydratase) (L-THA DH)
[liuE PA2011] 3-hydroxy-3-isohexenylglutaryl-CoA/hydroxy-methylglutaryl-CoA lyase (HIHG-CoA lyase) (HMG-CoA lyase) (EC 4.1.3.26) (EC 4.1.3.4) ((S)-3-hydroxy-3-methylglutaryl-CoA acetoacetate-lyase) (3-hydroxy-3-(4-methylpent-3-en-1-yl)glutaryl-CoA acetate-lyase)
[mutM fpg] Formamidopyrimidine-DNA glycosylase (Fapy-DNA glycosylase) (EC 3.2.2.23) (DNA-(apurinic or apyrimidinic site) lyase MutM) (AP lyase MutM) (EC 4.2.99.18)
[nth-1 R10E4.5] Endonuclease III homolog (CeNTH) (EC 3.2.2.-) (EC 4.2.99.18) (Bifunctional DNA N-glycosylase/DNA-(apurinic or apyrimidinic site) lyase) (DNA glycosylase/AP lyase)
[] Endonuclease V (EC 3.2.2.17) (DNA-(apurinic or apyrimidinic site) lyase) (AP lyase) (EC 4.2.99.18) (T4 pyrimidine dimer glycosylase) (T4-Pdg)
[hutIH BMEII0368] Bifunctional imidazolonepropionase/histidine ammonia-lyase [Includes: Imidazolonepropionase (EC 3.5.2.7) (Imidazolone-5-propionate hydrolase); Histidine ammonia-lyase (Histidase) (EC 4.3.1.3)]
[NTHL1 NTH1 OCTS3] Endonuclease III-like protein 1 (hNTH1) (EC 3.2.2.-) (EC 4.2.99.18) (Bifunctional DNA N-glycosylase/DNA-(apurinic or apyrimidinic site) lyase) (DNA glycosylase/AP lyase)
[APEX1 APE APE1 APEX APX HAP1 REF1] DNA-(apurinic or apyrimidinic site) lyase (EC 3.1.-.-) (EC 4.2.99.18) (APEX nuclease) (APEN) (Apurinic-apyrimidinic endonuclease 1) (AP endonuclease 1) (APE-1) (REF-1) (Redox factor-1) [Cleaved into: DNA-(apurinic or apyrimidinic site) lyase, mitochondrial]
[NTH1 At2g31450 T28P16.6] Endonuclease III homolog 1, chloroplastic (AtNTH1) (EC 3.2.2.-) (EC 4.2.99.18) (Bifunctional DNA N-glycosylase/DNA-(apurinic or apyrimidinic site) lyase 1) (DNA glycosylase/AP lyase 1)
[OGG1 MMH MUTM OGH1] N-glycosylase/DNA lyase [Includes: 8-oxoguanine DNA glycosylase (EC 3.2.2.-); DNA-(apurinic or apyrimidinic site) lyase (AP lyase) (EC 4.2.99.18)]
[NTH2 At1g05900 T20M3.18] Endonuclease III homolog 2, chloroplastic (AtNTH2) (EC 3.2.2.-) (EC 4.2.99.18) (Bifunctional DNA N-glycosylase/DNA-(apurinic or apyrimidinic site) lyase 2) (DNA glycosylase/AP lyase 2)
[hchA A8C65_13880 A9R57_25255 AKG99_20940 AMK83_16550 B7C53_22525 B9M99_11580 B9T59_01945 BJJ90_15205 BMT49_12710 BMT53_00170 BUE81_10670 BW690_17225 BZL69_29425 C2U48_24800 C5715_19445 C5N07_21380 C6669_19295 C7B06_02290 C7B07_03930 CDL37_00765 CG691_19145 CG705_13560 CG706_14580 CIJ94_05515 COD46_23180 CRD98_26150 D3I61_11545 DL800_09215 DNQ41_14245 DQE83_22775 DTL43_21780 DTL84_23375 DTM25_06080 EC95NR1_00961 ERS085379_01273 ERS085386_05041 HMPREF3040_01583 HW43_13705 NCTC10082_04431 NCTC10418_03071 NCTC10767_03558 NCTC11022_01867 NCTC11126_04427 NCTC11181_05650 NCTC12950_02263 NCTC13462_05714 NCTC8985_00529 NCTC9111_05933 NCTC9703_00277 PU06_24500 SAMEA3472055_03589 SAMEA3472056_01268 SAMEA3472070_00654 SAMEA3472080_04213 SAMEA3472090_03376 SAMEA3472110_00060 SAMEA3472112_00448 SAMEA3752372_00752 SAMEA3753106_00003 SAMEA3753391_00513 UN91_23615 WQ89_10695] Protein/nucleic acid deglycase HchA (EC 3.1.2.-) (EC 3.5.1.-) (EC 3.5.1.124) (Maillard deglycase)
[NTG1 OGG2 SCR1 YAL015C FUN33] Endonuclease III homolog 1 (EC 3.2.2.-) (EC 4.2.99.18) (Bifunctional DNA N-glycosylase/DNA-(apurinic or apyrimidinic site) lyase 1) (DNA glycosylase/AP lyase 1) (Endonuclease III-like glycosylase 1) (Redoxyendonuclease 1)
[Apex1 Ape Apex Ref1] DNA-(apurinic or apyrimidinic site) lyase (EC 3.1.-.-) (EC 4.2.99.18) (APEX nuclease) (APEN) (Apurinic-apyrimidinic endonuclease 1) (AP endonuclease 1) (REF-1) (Redox factor-1) [Cleaved into: DNA-(apurinic or apyrimidinic site) lyase, mitochondrial]
[APEX1 APE APEX BAP1 REF1] DNA-(apurinic or apyrimidinic site) lyase (EC 3.1.-.-) (EC 4.2.99.18) (APEX nuclease) (APEN) (Apurinic-apyrimidinic endonuclease 1) (AP endonuclease 1) (REF-1) (Redox factor-1) [Cleaved into: DNA-(apurinic or apyrimidinic site) lyase, mitochondrial]
[pyrG A6592_02570 A8M42_16405 A9R57_06965 AC067_22330 AC789_1c31020 ACN002_2797 ACN77_07080 ACN81_20385 ACU57_24415 ACU90_23015 AJ318_22735 AKG99_03555 AM270_00945 AM446_06950 AM464_05605 AM465_10605 AML07_12460 AML35_05300 APT94_17890 APU18_18535 APZ14_09290 ARC77_10140 AU473_08010 AUQ13_17535 AUS26_15660 AW059_10675 AW106_00665 AWP75_20610 AZZ83_003241 B1K96_20050 B7C53_10055 B9M99_21725 B9N33_09475 B9T59_19685 BB545_13920 BE963_03670 BEN53_16995 BET08_07180 BH694_13410 BHF46_05050 BHS81_16640 BHS87_15735 BIQ87_15835 BIU72_09520 BIZ41_16885 BJJ90_05265 BK248_12970 BK292_23205 BK334_11935 BK373_15870 BK375_10085 BK383_11680 BK400_05820 BMT49_17330 BMT53_21250 BMT91_11105 BN17_26661 BTQ04_11510 BTQ06_23845 BUE81_06975 BVL39_12970 BW690_04975 BWP17_05185 BXT93_24405 BZL31_00820 BZL69_02125 C1I57_04860 C2M16_17770 C2U48_20025 C3K24_08940 C4J69_11655 C4K41_05275 C4M78_00835 C5715_23540 C5N07_06155 C5P01_05005 C5P43_15935 C5P44_09340 C6669_14670 C6986_17750 C6B13_03370 C7235_05745 C7B02_19400 C7B06_11630 C7B07_14530 C7B08_01430 C9E25_03325 CA593_12975 CCZ14_04445 CCZ17_10850 CDL37_13440 CG691_07365 CG692_07005 CG705_05530 CG706_07860 CIJ94_12220 COD30_01795 COD46_07095 CR538_05495 CR539_18815 CRE06_03485 CRM83_26360 CSB64_15850 CT143_09630 CT146_00680 CV83915_03339 CVH05_06295 CWM24_00790 CWS33_03125 CXB56_08765 D0X26_06660 D1900_12730 D2183_19100 D2F89_14380 D3I61_16000 DD762_13665 DIV22_29760 DIV25_29790 DL545_05995 DL800_20505 DNQ41_18960 DNR41_08670 DQE83_04685 DS732_20695 DS966_06010 DTL43_09355 DTL84_00105 DTL90_02675 DTM10_03745 DTM25_22630 DTM27_13675 DTM45_13530 EC1094V2_904 EC3234A_48c00890 EC95NR1_02021 ECONIH1_15890 ECs3640 EL75_0914 EL79_0915 EL80_0918 ERS085365_02427 ERS085366_03042 ERS085374_03279 ERS085386_03410 ERS085416_02898 ERS139211_02072 ERS150873_02003 ERS150876_01467 FORC28_1110 GJ11_18025 HMPREF3040_01161 HW43_18180 JD73_16335 MJ49_17095 MS6198_30910 MS8345_02965 NCTC10082_03473 NCTC10090_04050 NCTC10418_01701 NCTC10764_00296 NCTC10766_00690 NCTC10767_02309 NCTC11022_02860 NCTC11112_00121 NCTC11181_03277 NCTC12950_01251 NCTC13125_04353 NCTC13127_01436 NCTC13462_04807 NCTC13846_01212 NCTC7152_00995 NCTC7927_01209 NCTC8500_01090 NCTC8960_03783 NCTC9007_03892 NCTC9010_01168 NCTC9036_01135 NCTC9037_01243 NCTC9045_01221 NCTC9050_04166 NCTC9058_00847 NCTC9062_02131 NCTC9075_01630 NCTC9077_01409 NCTC9081_05851 NCTC9117_01609 NCTC9119_01271 NCTC9434_01004 NCTC9706_03296 NCTC9775_04845 NCTC9777_02704 NCTC9969_01292 PU06_02080 RG28_07675 RK56_023165 SAMEA3472033_01264 SAMEA3472044_02272 SAMEA3472047_00339 SAMEA3472056_05455 SAMEA3472067_02540 SAMEA3472070_01673 SAMEA3472080_03155 SAMEA3472090_00131 SAMEA3472108_00527 SAMEA3472110_03462 SAMEA3472112_03722 SAMEA3472114_02432 SAMEA3472147_03296 SAMEA3484427_03298 SAMEA3484429_03415 SAMEA3484433_01660 SAMEA3484434_01581 SAMEA3485101_02257 SAMEA3485113_02257 SAMEA3752372_03639 SAMEA3752557_03040 SAMEA3752559_02995 SAMEA3752620_01282 SAMEA3753064_02287 SAMEA3753097_02219 SAMEA3753106_03183 SAMEA3753164_01192 SAMEA3753290_02847 SAMEA3753300_01107 SAMEA3753391_02580 SAMEA3753397_04005 SK85_03024 SY51_15605 UC41_20365 UN91_03645 WM48_14990 WQ89_10170 WR15_06090 YDC107_1339] CTP synthase (EC 6.3.4.2) (Cytidine 5'-triphosphate synthase) (Cytidine triphosphate synthetase) (CTP synthetase) (CTPS) (UTP--ammonia ligase)
[OGG1 YML060W YM9958.02] N-glycosylase/DNA lyase [Includes: 8-oxoguanine DNA glycosylase (EC 3.2.2.-); DNA-(apurinic or apyrimidinic site) lyase (AP lyase) (EC 4.2.99.18)]

Bibliography :
[30192043] Modular Enzymatic Cascade Synthesis of Vitamin B and Its Derivatives.
[22005738] Characterization of a thermostable methylaspartate ammonia lyase from Carboxydothermus hydrogenoformans.
[19670200] Alteration of the diastereoselectivity of 3-methylaspartate ammonia lyase by using structure-based mutagenesis.
[11796115] Insights into enzyme evolution revealed by the structure of methylaspartate ammonia lyase.
[11748244] The structure of 3-methylaspartase from Clostridium tetanomorphum functions via the common enolase chemical step.
[11717518] Crystallization and preliminary X-ray analysis of Citrobacter amalonaticus methylaspartate ammonia lyase.
[9830098] Cloning, nucleotide sequencing, and expression of the 3-methylaspartate ammonia-lyase gene from Citrobacter amalonaticus strain YG-1002.
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