HOME
login
history
all enzymes
BRENDA home
History
Information on EC 2.6.1.30 - pyridoxamine-pyruvate transaminase
for references in articles please use BRENDA:EC2.6.1.30Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
2.6.1.30 pyridoxamine-pyruvate transaminaseSpecify your search results
Word Map
- 2.6.1.30
- pyridoxal
-
transamination
- 5'-phosphate
- loti
-
mesorhizobium
- nabh4
-
4-oxidase
- 5'-deoxypyridoxal
- l-alanine
- pyridoxine
- analysis
The enzyme appears in viruses and cellular organisms
Synonyms
pyridoxamine-pyruvate aminotransferase, pyridoxamine-pyruvate transaminase, 
more
topPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
PPAT
pyridoxamine-pyruvate aminotransferase
pyridoxamine-pyruvate aminotransferase
pyridoxamine-2-oxoglutarate aminotransferase activity
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
pyridoxamine + pyruvate = pyridoxal + L-alanine
enzyme first binds pyridoxamine and then forms a Michaelis complex with the incoming pyruvate. The ketimine is formed through nucleophilic attack of the N-4' atom of pyridoxamine on the alpha-carbon atom of pyruvate, which is followed by the release of a water molecule. The stereospecific 1,3-prototropic shift between the ketimine and external aldimine via the quinonoid intermediate is accomplished through general base catalysis by Lys197. Pyridoxal and L-alanine are formed from the external aldimine and released from enzyme
pyridoxamine + pyruvate = pyridoxal + L-alanine
enzyme first binds pyridoxamine and then forms a Michaelis complex with the incoming pyruvate. The ketimine is formed through nucleophilic attack of the N-4' atom of pyridoxamine on the alpha-carbon atom of pyruvate, which is followed by the release of a water molecule. The stereospecific 1,3-prototropic shift between the ketimine and external aldimine via the quinonoid intermediate is accomplished through general base catalysis by Lys197. Pyridoxal and L-alanine are formed from the external aldimine and released from enzyme
-
pyridoxamine + pyruvate = pyridoxal + L-alanine
-
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
PATHWAY SOURCE
PATHWAYS
MetaCyc
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SYSTEMATIC NAME
IUBMB Comments
pyridoxamine:pyruvate aminotransferase
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
CAS REGISTRY NUMBER
COMMENTARY
9023-38-5
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
3-hydroxypyridine-4-aldehyde + L-alanine
3-hydroxy-4-aminomethylpyridine + pyruvate
-
-
-
r
omega-methylpyridoxal + L-alanine
omega-methylpyridoxamine + pyruvate
-
i.e. 3-hydroxy-5-hydroxymethyl-2-ethylpyridine-4-carboxaldehyde
-
r
pyridoxamine + 2-oxobutyrate
pyridoxal + (S)-2-aminobutyrate
poor substrate
-
r
(S)-2-aminobutyrate + pyruvate
?
(S)-2-aminobutyrate is a poor substrate
-
?
(S)-2-aminobutyrate + pyruvate
?
-
(S)-2-aminobutyrate is a poor substrate
-
?
pyridoxamine + pyruvate
pyridoxal + L-alanine
-
oxaloacetate and several other keto acids tested cannot replace pyruvate as amino group acceptor
-
r
pyridoxamine 5'-phosphate + pyruvate
pyridoxal 5'-phosphate + L-alanine
-
-
?
pyridoxamine 5'-phosphate + pyruvate
pyridoxal 5'-phosphate + L-alanine
-
-
?
additional information
?
-
-
the enzyme shows less than 0.5% of the activity of pyridoxamine towards pyridoxamine 5'-phosphate (3.3 mM) with pyruvate as the amino acceptor, the enzyme shows less than 0.5% of the activity of pyruvate towards 2-oxoglutarate, 3-hydroxypyruvate, indol-pyruvate, phenylpyruvate, 3-methyl-2-oxobutyrate and 4-hydroxyphenylpyruvate when they are used at 10 mM
-
?
additional information
?
-
the enzyme shows less than 0.5% of the activity of pyridoxamine towards pyridoxamine 5'-phosphate (3.3 mM) with pyruvate as the amino acceptor, the enzyme shows less than 0.5% of the activity of pyruvate towards 2-oxoglutarate, 3-hydroxypyruvate, indol-pyruvate, phenylpyruvate, 3-methyl-2-oxobutyrate and 4-hydroxyphenylpyruvate when they are used at 10 mM
-
?
additional information
?
-
-
the enzyme shows less than 0.5% of the activity of pyridoxamine towards pyridoxamine 5'-phosphate (3.3 mM) with pyruvate as the amino acceptor, the enzyme shows less than 0.5% of the activity of pyruvate towards 2-oxoglutarate, 3-hydroxypyruvate, indol-pyruvate, phenylpyruvate, 3-methyl-2-oxobutyrate and 4-hydroxyphenylpyruvate when they are used at 10 mM
-
?
additional information
?
-
-
no substrate: oxaloacetate, hydroxypyruvate and phenylpyruvate
-
?
additional information
?
-
-
not active with: 3-deoxypyridoxal, pyridine-4-aldehyde, O-methylpyridoxal, 4-nitrosalicylaldehyde
-
?
additional information
?
-
-
temperature-jump and stopped-flow kinetic investigation of the rate and mechanism of the reaction of 5'-deoxy-pyridoxal with the enzyme
-
?
additional information
?
-
-
determination of the active site stoichiometry and the pH dependence of the dissociation constant for 5'-deoxypyridoxal
-
?
additional information
?
-
-
enzyme is part of the degradative pathway for vitamin B6 compounds utilized by Pseudomonas sp. MA-1
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
additional information
?
-
-
enzyme is part of the degradative pathway for vitamin B6 compounds utilized by Pseudomonas sp. MA-1
-
-
?
pyridoxamine + pyruvate
pyridoxal + L-alanine
-
oxaloacetate and several other keto acids tested cannot replace pyruvate as amino group acceptor
-
r
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
pyridoxal 5'-phosphate
the bulky side chain of Glu68 interferes with the binding of the phosphate moiety of pyridoxal 5'-phosphate and makes the enzyme specific to pyridoxal
additional information
-
pyridoxal 5'-phosphate is not required for activity
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
4-Nitrosalicylaldehyde
-
inhibits pyridoxamine formation from pyridoxal + alanine
Pyridine-4-aldehyde
-
inhibits pyridoxamine formation from pyridoxal + alanine
additional information
-
hydroxylamine (10 mM), phenylhydrazine (1 mM) and sodium borohydride (1 mM) do not inactivate the enzyme
-
additional information
hydroxylamine (10 mM), phenylhydrazine (1 mM) and sodium borohydride (1 mM) do not inactivate the enzyme
-
additional information
-
not inhibitory: hydroxylamine, phenylhydrazine and sodium borohydride
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
17.2
2-oxoglutarate
M2T/Y35H/V70K/E212G mutant protein, pH 9.0, 30°C
additional information
additional information
Soil bacterium
-
effect of pH on kinetic parameters
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.234
2-oxoglutarate
M2T/Y35H/V70K/E212G mutant protein, pH 9.0, 30°C
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
8.5
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
70
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
Gram-negative bacillus isolate T2, 99.9% related to Ochrobactrum anthropi
-
-
brenda
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). PPAT_RHILO
Mesorhizobium japonicum (strain LMG 29417 / CECT 9101 / MAFF 303099)
393
0
41590
Swiss-Prot
-
A0A644VNR5_9ZZZZ
394
0
41343
TrEMBL
Secretory Pathway (Reliability: 3)
A0A2S6R093_9PROT
392
0
41646
TrEMBL
-
A0A645HL11_9ZZZZ
154
0
16653
TrEMBL
other Location (Reliability: 2)
A0A385ZTI8_9ACTN
365
0
38158
TrEMBL
-
A0A645DLQ6_9ZZZZ
254
0
27483
TrEMBL
other Location (Reliability: 1)
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
PDB
SCOP
CATH
UNIPROT
ORGANISM
Mesorhizobium japonicum (strain LMG 29417 / CECT 9101 / MAFF 303099)
Mesorhizobium japonicum (strain LMG 29417 / CECT 9101 / MAFF 303099)
Mesorhizobium japonicum (strain LMG 29417 / CECT 9101 / MAFF 303099)
Mesorhizobium japonicum (strain LMG 29417 / CECT 9101 / MAFF 303099)
Mesorhizobium japonicum (strain LMG 29417 / CECT 9101 / MAFF 303099)
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
41000
41589
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
homotetramer
tetramer
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
native enzyme, space group P43212, diffraction to 2.0 A resolution. Complexes with pyridoxamine, pyridoxal, and pyridoxyl-L-alanine at 1.7 A, 1.7 A, and 2.0 A resolution, respectively. Enzyme is a homotetramer and each subunit is composed of a large N-terminal domain, consisting of seven beta-sheets and eight alpha-helices, and a smaller C-terminal domain, consisting of three beta-sheets and four alpha-helices. The substrate pyridoxal is bound through an aldimine linkage to Lys197 in the active site. The carboxylate group of the substrate amino/keto acid is hydrogen-bonded to Arg336 and Arg345
addition of saturated ammonium sulfate solution to the concentrated protein solution until the first permanent turbidity appears, several days at 5°C
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
C198A
E68A
low pyridoxamine 5'-phosphate:pyruvate aminotransferase activity, decrease in activity towards pyridoxamine
E68G
low pyridoxamine 5'-phosphate:pyruvate aminotransferase activity, decrease in activity towards pyridoxamine
K197L
V70K
active site residue, increase in reactivity toward 2-oxoglutarate
E68A
-
low pyridoxamine 5'-phosphate:pyruvate aminotransferase activity, decrease in activity towards pyridoxamine
E68G
-
low pyridoxamine 5'-phosphate:pyruvate aminotransferase activity, decrease in activity towards pyridoxamine
C198A
enzyme shows the same specific activity as that of the wild type enzyme
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
30 - 80
17% and 3% of the maximal activity is observed at 30°C and 80°C, respectively
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
loss of activity within 12 h at 25°C in sodium phosphate buffer, but is stable in potassium buffer under the same conditions
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
partial, QA52 column chromatography and butyl-Toyopearl column chromatography
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
analysis
determination method for individual natural vitamin B6 compounds. Compounds are specifically converted into 4-pyridoxolactone by pyridoxal 4-dehydrogenase and coupling reactions involving pyridoxine 4-oxidase, pyridoxal 4-dehydrogenase, or pyridoxamine-pyruvate aminotransferase and pyridoxal 4-dehydrogenase. Application of method for analysis of food samples
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Wada, H.; Snell, E.E.
Enzymatic transamination pf pyridoxamine. II. Crystalline pyridoxamine-pyruvate transaminase
J. Biol. Chem.
237
133-137
1962
Pseudomonas sp.
brenda
Ayling, J.E.; Snell, E.E.
Relation of structure to activity of pyridoxal analogs as substrates for pyridoxamine pyruvate transaminase
Biochemistry
7
1626-1636
1968
Pseudomonas sp.
brenda
Ford, J.B.
Effect of pH and temperature on kinetic parameters of pyridoxamine-pyruvate transaminase
J. Ala. Acad. Sci.
49
16-30
1978
Soil bacterium
-
brenda
Gilmer, P.J.; McIntire, W.S.; Kirsch, J.F.
Pyridoxamine-pyruvate transaminase. 1. Determination of the active site stoichiometry and the pH dependence of the dissociation constant for 5-deoxypyridoxal
Biochemistry
16
5241-5246
1977
Pseudomonas sp.
brenda
Gilmer, P.J.; Kirsch, J.F.
Pyridoxamine-pyruvate transaminase. 2. Temperature-jump and stopped-flow kinetic investigation of the rates and mechanism of the reaction of 5-deoxypyridoxal with the enzyme
Biochemistry
16
5246-5253
1977
Pseudomonas sp.
brenda
Yanee, T.; Suwanna, N.; Sineenat, S.
Vitamin B6 degradation by pyridoxamine-pyruvate transaminase and pyridoxine 4-oxidase from Ochrobactrum anthropi- and Enterobacter cloacae-like bacteria
Science Asia
31
307-311
2005
Ochrobactrum anthropi
-
brenda
Yoshikane, Y.; Yokochi, N.; Ohnishi, K.; Hayashi, H.; Yagi, T.
Molecular cloning, expression and characterization of pyridoxamine-pyruvate aminotransferase
Biochem. J.
396
499-507
2006
Mesorhizobium loti, Mesorhizobium loti (Q988B8), Mesorhizobium loti MAFF303099
brenda
Yoshikane, Y.; Yokochi, N.; Yamasaki, M.; Mizutani, K.; Ohnishi, K.; Mikami, B.; Hayashi, H.; Yagi, T.
Crystal structure of pyridoxamine-pyruvate aminotransferase from Mesorhizobium loti MAFF303099
J. Biol. Chem.
283
1120-1127
2008
Mesorhizobium loti (Q988B8), Mesorhizobium loti, Mesorhizobium loti MAFF303099 (Q988B8)
brenda
Nishimura, S.; Nagano, S.; A Crai, C.; Yokochi, N.; Yoshikane, Y.; Ge, F.; Yagi, T.
Determination of individual vitamin B(6) compounds based on enzymatic conversion to 4-pyridoxolactone
J. Nutr. Sci. Vitaminol.
54
18-24
2008
Mesorhizobium loti (Q988B8)
brenda
Yoshikane, Y.; Tamura, A.; Yokochi, N.; Ellouze, K.; Yamamura, E.; Mizunaga, H.; Fujimoto, N.; Sakamoto, K.; Sawa, Y.; Yagi, T.
Engineering Mesorhizobium loti pyridoxamine-pyruvate aminotransferase for production of pyridoxamine with L-glutamate as an amino donor
J. Mol. Catal. B
67
104-110
2010
Mesorhizobium loti (Q988B8)
-
brenda
Huang, S.; Zhang, J.; Wu, M.; Wu, Q.; Huang, L.
Enzymatic transamination of pyridoxamine in tobacco plants
Plant Sci.
212
55-59
2013
Nicotiana tabacum
brenda
Select items on the left to see more content.
EXTERNAL LINKS (specific for EC-Number 2.6.1.30)
html completed
Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.
Information
