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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.
23-MAY-2018, entry version 92.
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, ENZYME
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: L-threo-3-methylaspartate = mesaconate +
NH(3). {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};
-!- ENZYME 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; IPR034390; Enolase-like_superfamily.
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.
SFLD; SFLDS00001; Enolase; 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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