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Information on EC 4.3.1.6 - beta-alanyl-CoA ammonia-lyase for references in articles please use BRENDA:EC4.3.1.6
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EC Tree
IUBMB Comments The reaction has only been demonstrated in the direction of addition of ammonia.
The expected taxonomic range for this enzyme is: Anaerotignum propionicum
Synonyms
ACL, ammonia-lyase, beta-alanyl coenzyme A, beta-alanyl coenzyme A ammonia-lyase, beta-alanyl-CoA:ammonia lyase 2,
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ammonia-lyase, beta-alanyl coenzyme A
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beta-alanyl coenzyme A ammonia-lyase
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beta-alanyl-CoA:ammonia lyase 2
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beta-alanyl-CoA = acryloyl-CoA + NH3
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beta-alanyl-CoA ammonia-lyase (acryloyl-CoA-forming)
The reaction has only been demonstrated in the direction of addition of ammonia.
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acryloyl-CoA + NH3
beta-alanyl-CoA
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r
acrylyl-CoA + NH3
beta-alanyl-CoA
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ir
additional information
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additional information
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the enzyme may play a role as precursor in the biosynthesis of beta-alanyl peptides such as anserine and carnosine
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enzyme is induced by beta-alanine. The enzyme is needed to bind acryloyl-CoA, in order to keep the toxic free form at a very low level
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additional information
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enzyme is induced by beta-alanine. The enzyme is needed to bind acryloyl-CoA, in order to keep the toxic free form at a very low level
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additional information
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additional information
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the enzyme may play a role as precursor in the biosynthesis of beta-alanyl peptides such as anserine and carnosine
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additional information
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enzyme is induced by beta-alanine. The enzyme is needed to bind acryloyl-CoA, in order to keep the toxic free form at a very low level
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additional information
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Q6KC22
enzyme is induced by beta-alanine. The enzyme is needed to bind acryloyl-CoA, in order to keep the toxic free form at a very low level
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NH4+
100 mM, 70% inhibition of NH3 elimination
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0.023
acryloyl-CoA
pH 7.5
0.21
beta-alanyl-CoA
pH 7.0
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25
beta-alanyl-CoA
pH 7.0
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brenda
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SwissProt
brenda
DSM 1682
SwissProt
brenda
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brenda
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F9EQ71_FUSNU
128
0
13948
TrEMBL
G8S6N0_ACTS5
Actinoplanes sp. (strain ATCC 31044 / CBS 674.73 / SE50/110)
121
0
12766
TrEMBL
C6JK85_FUSVA
127
0
13867
TrEMBL
E6PCI0_9ZZZZ
132
0
14383
TrEMBL
C3JBK8_POREA
Porphyromonas endodontalis (strain ATCC 35406 / BCRC 14492 / JCM 8526 / NCTC 13058 / HG 370)
130
0
14206
TrEMBL
D4CSU1_9FUSO
120
0
12898
TrEMBL
E6Q635_9ZZZZ
132
0
14351
TrEMBL
C2M973_9PORP
130
0
14037
TrEMBL
Q1D465_MYXXD
Myxococcus xanthus (strain DK 1622)
132
0
14250
TrEMBL
D5RCQ8_FUSN2
Fusobacterium nucleatum subsp. nucleatum (strain ATCC 23726 / VPI 4351)
128
0
13960
TrEMBL
F5SH43_9BACL
131
0
14206
TrEMBL
Q6KC22_CLOPR
144
0
16005
TrEMBL
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15999
5 * 15999, MALDI-TOF MS
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homohexamer
three dimers combine to a homohexamer
pentamer
5 * 15999, MALDI-TOF MS
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crystal structure of Acl in its apo-form at a resolution of 0.97 A as well as in complex with CoA at a resolution of 1.59 A. The structures reveal that the enyzme belongs to a superfamily of proteins exhibiting a so called 'hot dog fold' which is characterized by a five-stranded antiparallel beta-sheet with a long alpha-helix packed against it
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Stadtman, E.R.
The enzymatic synthesis of beta-alanyl coenzyme A
J. Am. Chem. Soc.
77
5765-5766
1955
Anaerotignum propionicum
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brenda
Herrmann, G.; Selmer, T.; Jessen, H.J.; Gokarn, R.R.; Selifonova, O.; Gort, S.J.; Buckel, W.
Two beta-alanyl-CoA:ammonia lyases in Clostridium propionicum
FEBS J.
272
813-821
2005
Anaerotignum propionicum, Anaerotignum propionicum (Q6KC22)
brenda
Heine, A.; Herrmann, G.; Selmer, T.; Terwesten, F.; Buckel, W.; Reuter, K.
High resolution crystal structure of Clostridium propionicum beta-alanyl-CoA: Ammonia lyase, a new member of the 'hot dog fold' protein superfamily
Proteins
82
2041-2053
2014
Anaerotignum propionicum (Q6KC22)
brenda
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4.3.1.6 beta-alanyl-CoA ammonia-lyase
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